Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
Putative 3-methyladenine DNA glycosylase
Belongs to the DNA glycosylase MPG family.
Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.
Complete sequence of Anaeromyxobacter sp. K.
ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA
ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC
Acetyl-CoA carboxylase carboxyltransferase subunit alpha
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).
ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Acetyl-CoA carboxylase carboxyltransferase subunit beta
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
ISOCITRATE DEHYDROGENASE KINASE/PHOSPHATASE
Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
4'-phosphopantetheinyl transferase domain
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Belongs to the P-Pant transferase superfamily. AcpS family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the acyl carrier protein (ACP) family.
Protein Spotlight; Slip sliding away - Issue 81 of April 2007
Required for adventurous-gliding motility (A motility), in response to environmental signals sensed by the frz chemosensory system. Forms ordered clusters that span the cell length and that remain stationary relative to the surface across which the cells move, serving as anchor points (focal, transient adhesion sites) that allow the bacterium to move forward. Clusters disassemble at the lagging cell pole.
In motile cells, localizes in ordered clusters spanning the cell length. In stalled cells, localizes at the leading cell pole.
Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.
Cysteine sulfenic acid (-SOH) intermediate
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL
N-acetyl-L-glutamate 5-phosphotransferase
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Bacterial exopeptidase dimerisation domain
Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines.
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Belongs to the peptidase M20A family. ArgE subfamily.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
3-phosphoshikimate 1-carboxyvinyltransferase
5-enolpyruvylshikimate-3-phosphate synthase
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
5-enolpyruvylshikimate-3-phosphate phospholyase
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Belongs to the chorismate synthase family.
Leucine Dehydrogenase, chain A, domain 1
BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE/SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC
Aminoacid dehydrogenase-like, N-terminal domain
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Belongs to the shikimate dehydrogenase family.
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Belongs to the succinylarginine dihydrolase family.
N-SUCCINYLGLUTAMATE 5-SEMIALDEHYDE DEHYDROGENASE
Succinylglutamic semialdehyde dehydrogenase
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Belongs to the aldehyde dehydrogenase family. AstD subfamily.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
ATP synthase alpha/beta chain, C-terminal domain
P-loop containing nucleotide triphosphate hydrolases
ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
C-terminal domain of alpha and beta subunits of F1 ATP synthase
N-terminal domain of alpha and beta subunits of F1 ATP synthase
P-loop containing nucleoside triphosphate hydrolases
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Belongs to the ATPase alpha/beta chains family.
ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
N-terminal domain of the delta subunit of the F1F0-ATP synthase
ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Belongs to the ATPase delta chain family.
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
Epsilon subunit of F1F0-ATP synthase N-terminal domain
Produces ATP from ADP in the presence of a proton gradient across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Belongs to the ATPase epsilon chain family.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
ATP synthase, gamma subunit, helix hairpin domain
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Belongs to the ATPase gamma chain family.
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Reversibly protonated during proton transport
Catalyzes the initial step in the conversion of aurachin C to aurachin B. Catalyzes the epoxidation of the C(2)-C(3) double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C(3) to C(4). Accepts both NADH and NADPH, but has a preference for NADH.
Mutant accumulates aurachin D and aurachin C and does not produce aurachin B and aurachin A.
EPIMERASE DOMAIN-CONTAINING PROTEIN-RELATED
Catalyzes the final step in the conversion of aurachin C to aurachin B. Catalyzes the reduction of 4-hydroxy-2-methyl-3-oxo-4-((2E,6E)-farnesyl)-3,4-dihydroquinoline-1-oxide to form 2-methyl-1-oxo-4-((2E,6E)-farnesyl)-3,4-dihydroquinoline-3,4-diol, which then undergoes a spontaneous dehydration to form aurachin B. Accepts both NADH and NADPH, but has a preference for NADH.
May be a dominant-negative inhibitor of eukaryotic actin polymerization.
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Belongs to the radical SAM superfamily. Biotin synthase family.
ATP-dependent dethiobiotin synthetase BioD
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Belongs to the dethiobiotin synthetase family.
CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 2-99
STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF BMC
Bacterial microcompartment protein homohexamer
The only hexameric shell protein in this bacterium, it forms the majority of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms a 40 nm artificial BMC with a molecular mass of 6.5 MDa. There are 60 BMC-H hexamers per BMC. The shell facets are 20-30 Angstroms thick (a single hexamer layer), with 1 of BMC-T trimers protruding to the exterior.
Homohexamer with a small central pore (PubMed:26617073, PubMed:28642439, PubMed:31075444, PubMed:30833088) (Probable). When purified protein is examined by atomic force microscopy it dynamically makes uniform patches about 35 Angstroms thick with hexamers in the same orientation (PubMed:26617073). In the BMC the concave side faces outward, with the N- and C-terminii exposed to the cytoplasm (PubMed:28642439).
Absolutely required for BMC formation; when deleted from an artificial operon (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) being expressed in E.coli, no BMC shells are made.
Artificial BMCs can be made in E.coli by expressing (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) or (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)). Cargo proteins can be targeted to this BMC (PubMed:24631000, PubMed:28642439). Artificial BMCs can be made by duplicating this gene with a 16 residue linker between the copies (making an artificial BMC-T). The shell assembles into balls with holes where the pentameric subunit would be, and can be used as a model to study assembly and permeability (PubMed:30901520). Additional changes to this protein place the N- and C-terminii in the interior of the shell (called CPH). Fusing proteins to the C-terminus of CPH allows targeting of cargo proteins to the lumen of the organelle composed of CPH, BMC-P and BMC-T1 (PubMed:31075444).
Belongs to the bacterial microcompartments protein family.
Forms larger hexamer patches, increases hexamer stacking.
STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS)
BACTERIAL MICROCOMPARTMENT VERTEX PROTEIN EUTN
Bacterial microcompartment shell vertex protein
Forms vertices in bacterial microcompartment (BMC) shells. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMC with a molecular mass of 6.5 MDa. There are 12 BMC-P pentamers per BMC. The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers protruding to the exterior.
Homopentamer. The base of the pyramid faces outward.
Not essential for BMC formation; when an artificial operon without BMC-P proteins (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816) is expressed in E.coli BMC shells are made.
Artificial BMCs can be made in E.coli by expressing (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) or (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)). Cargo proteins can be targeted to this BMC (PubMed:24631000, PubMed:28642439). BMC-H can be modified to place its N- and C-terminii in the interior of the shell (called CPH). Fusing proteins to the C-terminus of CPH allows targeting of cargo proteins to the lumen of the organelle composed of CPH, BMC-P and BMC-T1 (PubMed:31075444).
One of 3 BMC-P proteins in this bacteria, the others are Hoch_4425 and Hoch_4426.
STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF BMC
Bacterial microcompartment protein trimer-1
A minor component of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMCs with a molecular mass of 6.5 MDa. This protein does not form stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers protruding to the exterior.
Homotrimerizes to form a pseudohexamer (PubMed:28642439, PubMed:30833088, PubMed:26704697). Unlike its paralogs BMC-T2 and BMC-T3, the pseudohexamers do not stack. The concave side faces outward, with the N- and C-terminii exposed to the cytoplasm (PubMed:28642439, PubMed:30833088).
These proteins have 2 BMC domains which evolve independently of each other, giving the term pseudohexamer to the trimerized subunit. Although the homotrimer fills the approximate space of a BMC hexamer protein, the BMC-T trimers are more compact. Their universal presence in BMCs indicates their structural importance. The homohexamers form pores of at least 5 Angstroms in diameter.
Required for efficient BMC formation; when deleted from an artificial operon (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) being expressed in E.coli, a >10-fold decrease in BMC shells is seen.
Artificial BMCs can be made in E.coli by expressing (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) or (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)). Cargo proteins can be targeted to this BMC (PubMed:24631000, PubMed:28642439). BMC-H can be modified to place its N- and C-terminii in the interior of the shell (called CPH). Fusing proteins to the C-terminus of CPH allows targeting of cargo proteins to the lumen of the organelle composed of CPH, BMC-P and BMC-T1 (PubMed:31075444). This subunit has been modifed to bind a 4Fe-4S center, which is the first step in conferring electron-transfer function to BMCs (PubMed:26704697).
Binds a 4Fe-4S cluster, exposed on the concave face.
Bacterial microcompartment protein trimer-2
A minor component of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMCs with a molecular mass of 6.5 MDa. One of 2 stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of the stacked BMC-T trimers protruding to the exterior (PubMed:28642439, PubMed:30833088). The stacked trimers may serve as conduits to allow chemical flux across the protein shell, gated by Arg-70 which contacts Glu-69 in an adjacent subunit; they are flexible enough to play a role in accommodating variations in shell assembly (Probable).
Homotrimerizes to form a pseudohexamer. These stack, with the concave faces together, in purified bacterial microcompartments (BMC).
These proteins have 2 BMC domains which evolve independently of each other, giving the term pseudohexamer to the trimerized subunit. Although the homotrimer fills the approximate space of a BMC hexamer protein, the BMC-T trimers are more compact. Their universal presence in BMCs indicates their structural importance. The homohexamers form pores at least 5 Angstroms in diameter; in the stacked homohexamer 1 pore is open and the other is closed (PubMed:28642439). In the BMC the inner pore is fully or partially closed while the outer pore is closed (PubMed:30833088).
Not required for efficient BMC formation; when deleted from an artificial operon (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) being expressed in E.coli, normal BMC shells form.
Artificial BMCs can be made in E.coli by expressing (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) or (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)). Cargo proteins can be targeted to this BMC.
Bacterial microcompartment protein trimer-3
A minor component of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMCs with a molecular mass of 6.5 MDa. One of 2 stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of the stacked BMC-T trimers protruding to the exterior (PubMed:28642439, PubMed:30833088). The stacked trimers may serve as conduits to allow metabolite flux across the protein shell, gated by Arg-68 which contacts Glu-67 in an adjacent subunit; they are flexible enough to play a role in accommodating variations in shell assembly (Probable).
Homotrimerizes to form a pseudohexamer. These stack, with the concave faces together, with the concave faces together, in purified bacterial microcompartments (BMC).
These proteins have 2 BMC domains which evolve independently of each other, giving the term pseudohexamer to the trimerized subunit. Although the homotrimer fills the approximate space of a BMC hexamer protein, the BMC-T trimers are more compact. Their universal presence in BMCs indicates their structural importance. The homohexamers form pores of at least 5 Angstroms in diameter; in the stacked homohexamer both pores are closed (PubMed:28642439). In the BMC the inner pore is fully or partially closed while the outer pore is closed (PubMed:30833088).
Not required for efficient BMC formation; when deleted from an artificial operon (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) being expressed in E.coli, a 2-fold decrease in BMC formation is seen.
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEXES WITH HEME; EPOTHILONE D AND EPOTHILONE B
Involved in the biosynthesis of epothilones, macrolactones which have a narrow anti-fungal spectrum and microtubule-stabilizing activity. Catalyzes the epoxidation of epothilones C and D to epothilones A and B, respectively.
MUTAGENESIS OF 174-HIS-HIS-175; HIS-175 AND 249-GLY-GLY-250
REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR
Negative regulator of the carB operon in the dark. Binds specifically to the CarA operator, in the region around the carB promoter, which blocks access to the RNA polymerase.
Binds cobalamin (vitamin B12), but cobalamin is not required for CarA activity. Interaction with CarS prevents binding to DNA.
Forms homodimers or oligomers. Interacts with CarS.
The N-terminal region interacts with DNA and CarS, and the C-terminal region is involved in oligomerization and binding of cobalamin.
Deletion causes light-independent expression from the carB promoter.
Belongs to the CarA/CarH B12-binding photoregulator family.
Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
Carbamoyl phosphate synthetase, large subunit connection domain
Glutathione synthetase ATP-binding domain-like
Carbamoyl-phosphate synthase large chain
Carbamoyl-phosphate synthetase ammonia chain
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
MUTAGENESIS OF HIS-78; HIS-103; HIS-113 AND HIS-218
Identification of genes required for adventurous gliding motility in Myxococcus xanthus with the transposable element mariner.
MUTAGENESIS OF HIS-78; HIS-103; HIS-113; HIS-164; HIS-195 AND HIS-218
Plasmanylethanolamine desaturase involved in plasmalogen biogenesis in the membrane, required for light-induced carotenogenesis (PubMed:12519205, PubMed:18310035, PubMed:22267513, PubMed:31604315). Plasmalogens are glycerophospholipids with a hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1 position, and are involved in antioxidative and signaling mechanisms, most precisely in sensing photooxidative stress through singlet oxygen (PubMed:31604315). Participates in the light-dependent inactivation of the antisigma factor CarR (PubMed:12519205, PubMed:18310035). Mediates signaling by singlet oxygen, generated via photoexcited protoporphyrin IX (PubMed:22267513).
Histidine box-1 and -2 together with other histidine residues are essential for catalytic activity.
Deletion prevents the activation of the light inducible promoters of carQ, crtI and carB.
Belongs to the fatty acid desaturase CarF family.
Essential for plasmanylethanolamine desaturase activity
Impaired carotenoid synthesis caused by loss of plasmanylethanolamine desaturase activity.
No effect on plasmanylethanolamine desaturase activity.
Requires cobalamin (vitamin B12) for repressor activity. In the dark, binding of cobalamin to CarH induces its oligomerization, which enhances binding to the DNA and repressor activity. Light causes cobalamin photolysis and disruption of the cobalamin-CarH complex, which decreases interaction with DNA and allows transcription of the carB operon. Interaction with CarS also prevents binding to DNA.
Lack of activity, even in the presence of cobalamin. Retains the ability to interact with CarS.
Lack of activity. Decreases oligomerization.
RNA POLYMERASE SIGMA FACTOR FECI-RELATED
Sigma2 domain of RNA polymerase sigma factors
Sigma3 and sigma4 domains of RNA polymerase sigma factors
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor regulates genes for the light induced biosynthesis of carotenoids.
Belongs to the sigma-70 factor family. ECF subfamily.
Negative regulator of the carotenoid synthesis regulon. It is probably inactivated by protoporphyrin IX in the presence of blue light. Inactivation of CarR leads to loss of negative control over the carotenogenesis protein CarQ.
Involved in carotenoid biosynthesis. Antagonizes the transcriptional repressor proteins CarA and CarH by preventing their binding to DNA. Can also dissociate preformed CarA-DNA complexes. Does not bind DNA.
CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS2 3
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).
Homodimer, forms a heterotetramer with a Cas1 homodimer.
Operon expression begins by 6 hours after starvation has initiated development and is under strong negative regulation by DevS.
Part of an operon going from at least MXAN_7266 to MXAN_7259 that includes a CRISPR operon with transcription continuing into the pre-crRNA locus.
Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.
CRISPR-ASSOCIATED NUCLEASE/HELICASE CAS3-RELATED
Putative CRISPR-associated nuclease/helicase Cas3
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity.
In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.
In the central section; belongs to the CRISPR-associated helicase Cas3 family.
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Processes pre-crRNA into individual crRNA units (By similarity).
Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family. Subtype Myxan subfamily.
Energy-coupling factor transporter probable substrate-capture protein CbiM
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.
MUTAGENESIS OF SER-148; SER-149; SER-386; SER-412 AND SER-419
Esterase with broad substrate specificity, that may be involved in degradation of plant biomass present in the habitat of S.cellulosum. In vitro, displays acetyl esterase activity, aryl esterase activity, paraben esterase activity, carboxyl esterase activity, poly-3-hydroxybutyric acid (PHB) depolymerase activity, and a low feruloyl esterase activity. Does not possess any paraoxonase activity. Is able to bind to multiple substrate molecules simultaneously.
Comprises a single domain but contains five nucleophilic elbows. Each nucleophilic elbow forms a local active site with varied substrate specificities and affinities, thus possessing one or more enzyme activities.
Belongs to the carbohydrate esterase 1 (CE1) family.
About 30% decrease in acetyl esterase activity. Loss of PHB depolymerase activity.
About 20% decrease in aryl esterase activity. Loss of carboxyl esterase activity. Loss of PHB depolymerase activity.
About 90% decrease in aryl esterase activity. About 80% decrease in acetyl esterase activity. Nearly loss of paraben esterase activity. Loss of PHB depolymerase activity.
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.
TCP-1-like chaperonin intermediate domain
60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Belongs to the chaperonin (HSP60) family.
PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Protein-glutamate methylesterase/protein-glutamine glutaminase 2
Protein-glutamate methylesterase/protein-glutamine glutaminase 3
Protein-glutamate methylesterase/protein-glutamine glutaminase 4
Protein-glutamate methylesterase/protein-glutamine glutaminase 5
Protein-glutamate methylesterase/protein-glutamine glutaminase 6
CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED
CNF1/YfiH-like putative cysteine hydrolases
Probable chemoreceptor glutamine deamidase CheD 1
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Probable chemoreceptor glutamine deamidase CheD 2
Chloramphenicol acetyltransferase-like domain
Nonribosomal peptide synthetase, condensation domain
S-adenosyl-L-methionine-dependent methyltransferases
Involved in the synthesis of chondramides. Activates R-beta-tyrosine and probably phenylalanine.
Two module-bearing peptide synthase. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, condensation and epimerization (Probable).
Chondramides are secondary metabolites with antifungal and cytotoxic activity. They are non-ribosomally produced depsipeptides consisting of a polyketide chain and 3 amino acids (alanine, N-methyltryptophan and beta-tyrosine or alpha-methoxy-beta-tyrosine).
Belongs to the ATP-dependent AMP-binding enzyme family.
NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC
Molybdenum cofactor biosynthesis proteins
ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT
ATP-dependent Clp protease proteolytic subunit 1
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
ATP-dependent Clp protease proteolytic subunit 2
ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS
ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS1, CHLOROPLASTIC
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Binds to the N-terminal domain of the chaperone ClpA.
ClpX chaperone, C4-type zinc finger domain
ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL
ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED
Glucocorticoid receptor-like (DNA-binding domain)
ATP-dependent Clp protease ATP-binding subunit ClpX
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Belongs to the prokaryotic pantothenate kinase family.
Pantetheine-phosphate adenylyltransferase
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
BIFUNCTIONAL COENZYME A SYNTHASE-RELATED
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
A monovalent cation. Ammonium or potassium.
Belongs to the type III pantothenate kinase family.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
Belongs to the CobB/CobQ family. CobQ subfamily.
PROTOHEME IX FARNESYLTRANSFERASE, MITOCHONDRIAL
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
Dehydrogenates carotenes in the trans conformation: converts all-trans-zeta-carotene into all-trans-lycopene, one of the last dehydrogenation steps of lycopene biosynthesis.
Belongs to the carotenoid/retinoid oxidoreductase family.
zeta-carotene-forming phytoene desaturase
Dehydrogenates carotenes in the cis conformation: has cis-to-trans isomerase activity and mediates dehydrogenation of cis-phytoene, producing zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of 2 double bonds at the C-11 and C-11' positions of phytoene.
CRISPR-associated endonuclease Cas1, C-terminal domain
CRISPR-associated endonuclease Cas1, N-terminal domain
CRISPR-associated exonuclease Cas4/endonuclease Cas1 fusion
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The Cas4 region acts as a ssDNA exonuclease, while the Cas1 region acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).
Homodimer, forms a heterotetramer with a Cas2 homodimer.
In the N-terminal section; belongs to the CRISPR-associated exonuclease Cas4 family.
In the C-terminal section; belongs to the CRISPR-associated endonuclease Cas1 family.
Cell surface-associated intercellular C-signal
Cell-cell signaling protein required for fruiting body formation, a multicellular developmental program that is induced in response to starvation (PubMed:2107980, PubMed:2118510, PubMed:10220413, PubMed:11298283, PubMed:12923062). Necessary for rippling, cellular aggregation, spore differentiation and for gene expression that is initiated after 6 hours of starvation (PubMed:2107980, PubMed:11298283). In starving cells, the C-signal directly induces aggregation and sporulation, which are induced at distinct threshold levels of C-signaling (PubMed:11298283). Contact with C-signaling induces cells to glide with high speed and low stop and reversal frequencies toward aggregation centers (PubMed:10220413). The C-signal acts as a morphogen and induces distinct events at distinct threshold levels (PubMed:11298283). A regulated increase in the level of C-signaling during development ensures the correct temporal order of aggregation and sporulation (PubMed:11298283).
Synthesized as a precursor protein (p25), which is cleaved after secretion to generate the mature active C-signal (p17) (PubMed:12923062). The p25 precursor purified from M.xanthus cells does not display C-signal activity (PubMed:12923062).
The CsgA precursor protein (p25) and the mature C-signal protein (p17) are both associated with the outer membrane (PubMed:12923062). Proper localization of p17 to the outer membrane depends on correct export and localization of p25 (PubMed:12923062).
Expression increases throughout development, reaching its peak during sporulation (PubMed:2152896, PubMed:1372277). Transcription is inhibited by excess nutrients and stimulated by peptidoglycan components and the B signal (PubMed:1372277). The csgA upstream region appears to process information concerning the levels of nutrients, peptidoglycan components and the B signal (PubMed:1372277). In the absence of nutrients, a region extending 400 bp upstream from the start site is necessary for development and maximal expression (PubMed:1372277). In the presence of low levels of nutrients, a region extending approximately 930 bp upstream is essential for the same tasks (PubMed:1372277).
The mature C-signal (p17) is derived from the precursor sequence (p25) by proteolytic cleavage (PubMed:12923062, PubMed:18854146). The subtilisin-like protease PopC is directly responsible for cleavage of p25 to p17 (PubMed:18854146). The cleavage site is probably located between amino acid residues 60 and 68 in p25 (PubMed:12923062).
Mutants fail to form proper multicellular aggregates, to differentiate from rod-shaped cells to environmentally resistant spores and to express development-specific genes.
Overproduction of the CsgA protein has dramatic effects on the developmental program: the rippling stage is bypassed, aggregation occurs prematurely and results in the formation of many small fruiting bodies, sporulation occurs prematurely, C-signal-dependent gene expression is induced prematurely, and aggregation and sporulation are uncoupled (PubMed:11298283). Reduced synthesis of the CsgA protein causes delayed aggregation, reduced sporulation and the formation of large fruiting bodies (PubMed:11298283).
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-424
ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED
Inhibited by adenosine. Activated by GTP.
Belongs to the adenylyl cyclase class-3 family.
It is uncertain whether Met-1 or Met-2 is the initiator.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-350
ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC
In the C-terminal section; belongs to the adenylyl cyclase class-3 family.
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
Catalyzes the synthesis of activated sulfate.
Adenine nucleotide alpha hydrolases-like
With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Heterodimer composed of CysD, the smaller subunit, and CysN.
Belongs to the PAPS reductase family. CysD subfamily.
SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED
Nitrite and sulphite reductase 4Fe-4S domain-like
Nitrite/Sulfite reductase N-terminal domain-like
Sulfite reductase [NADPH] hemoprotein beta-component
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Probable inorganic carbon transporter subunit DabA 1
Part of an energy-coupled inorganic carbon pump.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.
Probable inorganic carbon transporter subunit DabA 2
4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.
4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL
4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
4-hydroxy-tetrahydrodipicolinate reductase
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.
AEROBIC C4-DICARBOXYLATE TRANSPORT PROTEIN
Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane.
Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.
METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Belongs to the uroporphyrinogen decarboxylase family.
Binds 2 magnesium or manganese ions per subunit.
Belongs to the D-alanine--D-alanine ligase family.
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Belongs to the phosphopentomutase family.
PURINE NUCLEOSIDE PHOSPHORYLASE DEOD-TYPE
Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Belongs to the PNP/UDP phosphorylase family.
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Associates with the 50S ribosomal subunit.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
SIMILARITY TO BETA/GAMMA-CRYSTALLIN FAMILY
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-89 IN COMPLEX WITH CALCIUM
Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.
Has a two-domain beta-structure, folded into four very similar Greek key motifs. The N-terminal domain (NPS) binds 2 calcium ions.
Belongs to the beta/gamma-crystallin family.
Localized at the outermost layer of myxospores.
Has a two-domain beta-structure, folded into four very similar Greek key motifs.
CRISPR-associated protein Cas7/Cst2/DevR
CRISPR-associated protein Cas7/Cst2/DevR, subtype I-B/Tneap
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).
Has a role in fruiting body development, sporulation and aggregation.
Operon expression begins by 6 hours after starvation has initiated development and is under strong negative autoregulation.
Essential for sporulation, decreases sporulation 100 to 1000-fold, aggregation is defective.
Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-B/Tneap subfamily.
Essential for sporulation, decreases sporulation 100 to 1000-fold. Negative autoregulation by this gene product relies on DNA both upstream and downstream of the operon's promoter.
Belongs to the CRISPR-associated protein Cas5 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 346-570
CRISPR-associated protein Cas8a1/Csx13, Myxan subtype
Functions in an unknown fashion to stimulate transcription of fruA independently of the intracellular A- and E-developmental signals.
Decreases sporulation 1000 to 10000-fold, aggregation is delayed. Delays for C-signal-dependent methylation of FrczCD and impairs fruA transcription. This mutant should not have polar effects on downstream genes.
Belongs to the CRISPR-associated protein Cas8a1/Csx13 family. Myxan subtype subfamily.
2-IMINOBUTANOATE/2-IMINOPROPANOATE DEAMINASE
2-IMINOBUTANOATE/2-IMINOPROPANOATE DEAMINASE RIDA
Bacterial DNA polymerase III alpha subunit, thumb domain
DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.
Belongs to the DNA polymerase type-C family. DnaE2 subfamily.
DNA primase, catalytic core, N-terminal domain
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Heat shock protein DnaJ, cysteine-rich domain
Urease metallochaperone UreE, N-terminal domain
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Heat shock protein 70kD (HSP70), C-terminal subdomain
Heat shock protein 70kD (HSP70), peptide-binding domain
Potential chaperone for other proteins involved in social motility.
By stress conditions e.g. heat shock (By similarity).
Belongs to the heat shock protein 70 family.
DNA ligase, ATP-dependent, N-terminal domain
ATP-dependent DNA ligase DNA-binding domain
DNA ligase/mRNA capping enzyme, catalytic domain
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Belongs to the ATP-dependent DNA ligase family.
5' to 3' exonuclease, C-terminal subdomain
CHROMOSOME TRANSMISSION FIDELITY FACTOR 18
Polydeoxyribonucleotide synthase [NAD(+)]
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Gly-cisPro motif, important for rejection of L-amino acids
DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE
1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC
1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED
1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC
Thiamin diphosphate-binding fold (THDP-binding)
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Binds 1 thiamine pyrophosphate per subunit.
Belongs to the transketolase family. DXPS subfamily.
Catalyzes the cyclization of farnesyl diphosphate (FPP) to 10-epi-cubebol. Is also responsible for the formation of many other sesquiterpenes, mainly cadalanes and cubebanes, including 1,10-di-epi-cubebol and the cadalanes delta-cadinene, T-cadinol and alpha-cadinol.
Dehydroquinate synthase-like - alpha domain
Catalyzes the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone.
Belongs to the sugar phosphate cyclases superfamily. EEVS-like family.
Elongation Factor G (Translational Gtpase), domain 3
RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
DNA helicase RuvA subunit, C-terminal domain
Elongation factor Ts, dimerisation domain
Elongation factor Ts (EF-Ts), dimerisation domain
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Involved in Mg(2+) ion dislocation from EF-Tu
EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-396
STRUCTURE BY ELECTRON MICROSCOPY (2.40 ANGSTROMS)
Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells about 21 nm in diameter. Small pores form at, or close to, the 2-, 3-, and 5-fold symmetry axes. Data analysis suggests the 5-fold pores open and close with maximal and minimal aperatures of 15 and 5 Angstroms. Cargo protein Fer (ferritin-like protein, probably stores iron) is targeted to the interior via its C-terminal extension; empty intact shells can be isolated in the absence of cargo protein.
This encapsulin nanocompartment is formed by 60 subunits; monomers form 12 pentamers which assemble to form shells. Shells are loaded with 4 encapsulated ferritin-like protein decamers (EncFtn) in a tetrahedral arrangement. A 3 nm gap is consistently seen between the shell and the cargo.
Belongs to the encapsulin family. Family 1 subfamily.
STRUCTURE BY ELECTRON MICROSCOPY (4.60 ANGSTROMS) OF 1-287
Shell component of a type 1, iron-storage encapsulin nanocompartment. Encapsulin nanocompartments are 32 nm in diameter with an iron- and phosphorus-rich core (4Fe:1P) about 24 nm in diameter. Upon expression in E.coli most particles are 32 nm, 20% are 18 nm. The core is filled with an average of 14 dense granules, 5-6 nm in diameter that are not evenly distributed. Each nanocompartment is estimated to hold 30,000-35,000 Fe atoms (PubMed:25024436, PubMed:31194509). The minor proteins EncB, EncC and EncD probably lie against the interior face of the nanocompartment (Probable).
The 32 nm encapsulin nanocompartment is formed by 180 subunits; monomers form pentamers which assemble to form shells. There are 36 pores where the pentamers meet as well as 3-fold axis channels and dimer channels. The N-terminus of the protein is inside the shell.
Part of the MXAN_3553-MXAN_3554-MXAN_3555-encA operon (PubMed:19996678). Expression is induced by amino acid starvation (at protein level). Not present in spores (at protein level) (PubMed:25024436).
Has 3 domains; a discontinuous peripheral domain (P), an elongated loop (E) and the discontinuous axial domain (A).
Does not form fruiting bodies (PubMed:19996678). Decreased survival when grown under oxidative stress (0.5 mM H2O2) (PubMed:25024436).
The encapsulin and a cargo construct (an encB-encC-encD fusion) can be overexpressed in E.coli and in human HEK293T cells. In HEK293T in the presence of 0.5 M ferrous ammonium sulfate nanocompartments can be detected and used as cell markers. Coexpression of this nanocompartment with a larger nanocompartment from Q.thermotolerans (AC A0A0F5HPP7) allows expression of different sized iron-rich particles. The encapsulin shell proteins do not seem to mix.
Shows substantial structural similarity to gp5 of the HK97 viral capsid, and while the sequence homology is weak, it suggests this protein may have evolved from a viral capsid protein.
Encapsulin nanocompartment cargo protein EncB
Cargo protein of a type 1 encapsulin nanocompartment. May help nucleate Fe atoms in the interior of the encapsulin nanocompartment (Probable). Present in about 36 copies/encapsulin nanocompartment (PubMed:25024436).
Probably lies against the interior face of the nanocompartment.
The encapsulin and a cargo construct (an encB-encC-encD fusion) can be overexpressed in E.coli and in human HEK293T cells. In HEK293T in the presence of 0.5 M ferrous ammonium sulfate nanocompartments can be detected and used as cell markers. Coexpression of this nanocompartment with a larger nanocompartment from Q.thermotolerans (AC A0A0F5HPP7) allows of expression of different sized iron-rich particles. The encapsulin shell proteins are not seen to mix.
Belongs to the ferritin-like superfamily.
Encapsulin nanocompartment cargo protein EncC
Cargo protein of a type 1 encapsulin nanocompartment. May help nucleate Fe atoms in the interior of the encapsulin nanocompartment (Probable). Present in about 92 copies/encapsulin nanocompartment (PubMed:25024436).
Encapsulin nanocompartment cargo protein EncD
Cargo protein of a type 1 encapsulin nanocompartment. May help nucleate Fe atoms in the interior of the encapsulin nanocompartment (Probable). Present in about 47 copies/encapsulin nanocompartment (PubMed:25024436).
Necessary for normal cell division and for the maintenance of normal septation.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.
Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene eremophilene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cation. The only accepted substrate is farnesyl diphosphate (FPP).
The Asp-Asp-Xaa-Xaa-Asp (DDXXD) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Catalyzes the conversion of sedoheptulose 7-phosphate to 2-epi-valiolone, which may serve as an alternative precursor for aminocyclitol biosynthesis.
Binds 1 divalent metal cation per subunit. Co(2+) is the preferred cofactor.
Belongs to the sugar phosphate cyclases superfamily. EVS family.
Fructose-1,6-Bisphosphatase, subunit A, domain 1
SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 3
(3R)-HYDROXYMYRISTOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE
3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE
Thioesterase/thiol ester dehydrase-isomerase
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Belongs to the thioester dehydratase family. FabZ subfamily.
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-97
Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like ferroxidase that converts Fe(2+) to Fe(3+) iron inside the encapsulin nanocompartment (PubMed:30837306, PubMed:35080974). Mineralized Fe(3+) is released to the exterior of the decameric complex for deposition in the encapsulin nanocompartment. In solution the decamer binds 10-15 iron cations; in the encapsulin nanocompartment the decamer can bind up to 48 ions, perhaps via its internal channel, and on its exterior. The cargo-loaded nanocompartment maximally sequesters up to 4150 Fe ions (By similarity).
The ferroxidase activity is inhibited by zinc.
Forms dimers at all pH tested; under acidic conditions formes decamers. The N-terminal domain (residues 1-97) crystallizes as a decameric ring (PubMed:30837306). Four decamers are loaded in the encapsulin nanocompartment in a tetrahedral arrangement. A 3 nm gap is consistently seen between the shell and the cargo. The target peptide extends away from the decameric ring, to allow binding to the interior of the encapsulin nanocompartment shell (PubMed:35080974).
The decamer has negatively charged patches on its exterior, and a negatively charged tunnel at the center, the charges are probably metal-binding sites.
Belongs to the ferritin-like superfamily. EncFtn family.
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
Belongs to the Fe(2+)-trafficking protein family.
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod.
FLAGELLAR P-RING PERIPLASMIC PROTEIN FLGI
Serine-tRNA synthetase, tRNA binding domain
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Belongs to the flotillin-like FloA family.
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Na(+) is not transported, but it plays an essential structural role and its presence is essential for fluoride channel function.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC
C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
CHEMOTAXIS SENSOR HISTIDINE KINASE-RELATED
Necessary for proper aggregation of cells to form fruiting bodies. FRZ genes define a system of signal transduction analogous to the enterobacterial chemotaxis systems.
Methyl-accepting chemotaxis protein (MCP) signaling domain
Methyl-accepting taxis protein necessary for the proper aggregation of cells to form fruiting bodies. Frz genes define a system of signal transduction analogous to the enterobacterial chemotaxis systems.
Methylated. Saturated fatty acids capric acid and lauric acid stimulate methylation. Short-chain alcohols, such as isoamyl alcohol, and some other solvents cause demethylation.
Belongs to the methyl-accepting chemotaxis (MCP) protein family.
Histidine kinase-like ATPase, C-terminal domain
ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Histidine-containing phosphotransfer domain, HPT domain
FrzE is involved in a sensory transduction pathway that controls the frequency at which cells reverse their gliding direction. FrzE seems to be capable of autophosphorylating itself on a histidine residue and then to transfer that group to an aspartate residue in the C-terminal part of the protein.
Chemotaxis receptor methyltransferase CheR, N-terminal domain
CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN
This methyltransferase is one of the proteins required for the normal aggregation of M.xanthus cells during fruiting body formation. It is also a component of a sensory transduction pathway that controls the frequency at which cells reverse their gliding direction. It may methylate FrzCD to form gamma-glutamyl methyl ester residues.
Probable methylesterase (By similarity). Required for the normal aggregation of M.xanthus cells during fruiting body formation. It is also a component of a sensory transduction pathway that controls the frequency at which cells reverse their gliding direction. It may remove the methyl group from the gamma-glutamyl methyl ester residues in FrzCD.
Domain 2, N(10)-formyltetrahydrofolate synthetase
Formyltetrahydrofolate synthetase, domain 3
Belongs to the formate--tetrahydrofolate ligase family.
ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1
ATP-dependent zinc metalloprotease FtsH 1
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
ATP-dependent zinc metalloprotease FtsH 2
ATP-dependent zinc metalloprotease FtsH 3
ATP-dependent zinc metalloprotease FtsH 4
Belongs to the FtsQ/DivIB family. FtsQ subfamily.
Myxococcus xanthus fumarate hydratase, major proteosome subunit, and acyl-CoA oxidase genes.
ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the amidase family. GatA subfamily.
GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Glu-tRNAGln amidotransferase C subunit, N-terminal domain
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
MUTAGENESIS OF TYR-45; HIS-99 AND HIS-183
PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3
Homodimeric domain of signal transducing histidine kinase
Heme-based oxygen-sensor histidine kinase
Member of the two-component regulatory system GcHK/Anae109_2439. Autophosphorylates in response to oxygen availability, and then transfers the phosphate group to a conserved Asp residue in the receiver domains of the cognate response regulator Anae109_2439, resulting in its activation.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Gas or ligand binding and heme iron redox state regulate the histidine kinase activity: heme-free AfGcHK and the heme Fe(II) complex are less active forms, whereas the heme Fe(III)-OH(-), Fe(III)-CN(-), Fe(III)-imidazole, Fe(II)-CO, and Fe(II)-O(2) complexes are active forms. The activation of the functional domain seems to be dependent on the formation of a six-coordinate low-spin heme iron complex. Mg(2+) ions, and to a lesser extent, Mn(2+) ions, enhance the autophosphorylation reaction, although the presence of a divalent metal ion does not appear to be essential for the reaction. Co(2+), Ni(2+), Zn(2+), and Cd(2+) totally inhibit autophosphorylation activity.
kcat is 1.1 min(-1) for the autophosphorylation reaction with the Fe(III)-OH(-) bound form of the enzyme. kcat is 1.2 min(-1) with the Fe(III)-CN(-) bound form of the enzyme. kcat is 1.1 min(-1) with the Fe(III)-imidazole bound form of the enzyme. kcat is 1.0 min(-1) with the Fe(II)-O(2) bound form of the enzyme. kcat is 1.0 min(-1) with the Fe(II)-CO bound form of the enzyme. kcat is 0.4 min(-1) with the Fe(II) bound form of the enzyme. kcat is 0.3 min(-1) with the heme-free form of the enzyme. The presence of the cognate response regulator (RR) protein significantly reduces the enzyme affinity for ATP.
18.9 uM for ATP (with the Fe(III)-OH(-) bound form of the enzyme)
35.4 uM for ATP (with the Fe(III)-CN(-) bound form of the enzyme)
23.8 uM for ATP (with the Fe(III)-imidazole bound form of the enzyme)
23.0 uM for ATP (with the Fe(II)-O(2) bound form of the enzyme)
357.0 uM for ATP (with the Fe(II)-CO bound form of the enzyme)
78 uM for ATP (with the Fe(II) bound form of the enzyme)
33.6 uM for ATP (with the heme-free form of the enzyme)
Optimum pH is around 11.0 for the autophosphorylation reaction with the Fe(III)-OH(-) bound form of the enzyme. At pH 8.0, displays 75% of the optimal rate. Is inactive below pH 5.5 and above pH 12.7.
Consists of two domains: an N-terminal heme-based oxygen-sensor domain, and a C-terminal catalytic domain that exhibits histidine kinase activity (PubMed:21852234). The coordination and oxidation state of the sensor domain heme iron profoundly affect the enzyme's catalytic activity (PubMed:26212354).
3.5-fold increase in O(2) dissociation rate constant. No effect on O(2) association rate constant.
80-fold increase in O(2) dissociation rate constant. No effect on O(2) association rate constant.
34-fold increase in O(2) dissociation rate constant. No effect on O(2) association rate constant.
Loss of heme-binding ability. 4-fold decrease in autophosphorylation reaction rate and 2-fold decrease in affinity for ATP.
Loss of autophosphorylation. Does not significantly alter the O(2) and CO binding kinetic values.
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.
GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Probable glycine dehydrogenase (decarboxylating) subunit 1
Glycine cleavage system P-protein subunit 1
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits.
Belongs to the GcvP family. N-terminal subunit subfamily.
GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC
STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC
UDP-Glycosyltransferase/glycogen phosphorylase
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
Phosphotransferase system, lactose/cellobiose-type IIA subunit
ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE
(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase
Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
Belongs to the glycosyl hydrolase 13 family. GlgE subfamily.
Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3
Alpha-D-phosphohexomutase, C-terminal domain
PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Belongs to the phosphohexose mutase family.
UDP-N-acetylglucosamine pyrophosphorylase
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
Ribonuclease Z/Hydroxyacylglutathione hydrolase-like
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Inhibited by fructose 1,6-bisphosphate (FBP).
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Plays an important role in substrate specificity
GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC
6-phosphogluconate dehydrogenase C-terminal domain-like
Glycerol-3-phosphate dehydrogenase [NAD(P)+]
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
BPG-independent phosphoglycerate mutase, domain B
2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE
2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Belongs to the BPG-independent phosphoglycerate mutase family.
Transcription elongation factor, GreA/GreB, C-terminal domain
Transcription elongation factor, GreA/GreB, N-terminal domain
GreA transcript cleavage protein, N-terminal domain
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Head domain of nucleotide exchange factor GrpE
Coiled-coil domain of nucleotide exchange factor GrpE
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE
GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED
Glutamate-1-semialdehyde aminotransferase
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
Vitiosangium phaeum 53X41T novel myxobacteria isolated from forest.
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 2-266
Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Expression of bGSDM and the neighboring protease gene (Ga0334635_1659) is toxic in E.coli (PubMed:35025633). Cleavage of this precursor by its dedicated protease releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and triggering cell death (By similarity).
Pore-forming protein that causes membrane permeabilization via a pyroptosis-like activity. Makes ring-like pores when released.
The full-length protein before cleavage is inactive: intramolecular interactions between the N-terminal domain and the C-terminal region as well as the lipid modification, mediate autoinhibition (Probable). The pyroptosis-like-inducing activity is carried by the released N-terminal domain (Gasdermin bGSDM, N-terminus) (By similarity).
Forms large, probably homooligomeric ring-shaped pores when inserted in membranes.
The N-terminus has marked structural similarity to the mammalian gasdermin N-terminal domain. The C-terminal region wraps around the twisted beta sheet core, probably stabilizing the inactive state.
Palmitoylation helps stabilize the inactive state; may self palmitoylate.
Full-length, unmodified protein expressed in E.coli.
Full-length, palmitoylated protein expressed in E.coli.
Full-length, modified protein expressed in E.coli.
Belongs to the bacterial gasdermin family.
Increased cell growth arrest upon induction.
Belongs to the ZIP transporter (TC 2.A.5) family.
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Belongs to the type II topoisomerase GyrB family.
Glutamyl-tRNA reductase, N-terminal domain
Glutamyl tRNA-reductase catalytic, N-terminal domain
Glutamyl tRNA-reductase dimerization domain
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Belongs to the glutamyl-tRNA reductase family.
Porphobilinogen deaminase, C-terminal domain
Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Binds 1 dipyrromethane group covalently.
The porphobilinogen subunits are added to the dipyrromethane group.
Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.
Belongs to the homogentisate dioxygenase family.
ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Heteromultimer composed of HisG and HisZ subunits.
Lacks the C-terminal regulatory region which is replaced by HisZ.
Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF
IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H
Imidazole glycerol phosphate synthase subunit HisF
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
ATP phosphoribosyltransferase regulatory subunit
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one.
Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily.
Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (HmuV), two transmembrane proteins (HmuU) and a solute-binding protein (HmuT).
Belongs to the ABC transporter superfamily. Heme (hemin) importer (TC 3.A.1.14.5) family.
K(+)-INSENSITIVE PYROPHOSPHATE-ENERGIZED PROTON PUMP
Putative K(+)-stimulated pyrophosphate-energized sodium pump
Membrane-bound sodium-translocating pyrophosphatase
Pyrophosphate-energized inorganic pyrophosphatase
Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-stimulated subfamily.
HEAT-INDUCIBLE TRANSCRIPTION REPRESSOR HRCA
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
Belongs to the ClpX chaperone family. HslU subfamily.
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Allosterically activated by HslU binding.
Belongs to the peptidase T1B family. HslV subfamily.
Heat shock protein 90, C-terminal domain
Molecular chaperone. Has ATPase activity.
Belongs to the heat shock protein 90 family.
Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Composite domain of metallo-dependent hydrolases
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Belongs to the metallo-dependent hydrolases superfamily. HutI family.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Chimera. Seems to include DNA from another gene.
TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.
Translation initiation factor IF- 2, domain 3
TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL
TRANSLATION INITIATION FACTOR IF-2-RELATED
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Translation initiation factor 3 (IF-3), C-terminal domain
Translation initiation factor 3 (IF-3), N-terminal domain
TRANSLATION INITIATION FACTOR IF-3, MITOCHONDRIAL
Translation initiation factor IF3, C-terminal domain
Translation initiation factor IF3, N-terminal domain
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
The 66 residues C-terminal tail is not present in other species.
Needed for vegetative and developmental functions, but not for viability
In strain: DK429 and DK439; causes defects in fruiting body development and in sporulation.
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Heterodimer of an alpha and a beta chain.
Belongs to the bacterial histone-like protein family.
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. It is necessary for normal cell growth and the production of carotenoids in response to light.
KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL
Alpha-keto-beta-hydroxylacyl reductoisomerase
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Belongs to the ketol-acid reductoisomerase family.
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Homodimer. Forms a heterotetramer with IscU, interacts with other sulfur acceptors.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
4-diphosphocytidyl-2C-methyl-D-erythritol synthase
Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
In the C-terminal section; belongs to the IspF family.
Positions MEP for the nucleophilic attack
4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Belongs to the GHMP kinase family. IspE subfamily.
4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain
4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN
Non-canonical purine NTP pyrophosphatase
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
RdgB/HAM1 family non-canonical purine NTP pyrophosphatase
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Microbial and mitochondrial ADK, insert 'zinc finger' domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
POTASSIUM-TRANSPORTING ATPASE POTASSIUM-BINDING SUBUNIT
ATP phosphohydrolase [potassium-transporting] A chain
Potassium-binding and translocating subunit A
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
The system is composed of three essential subunits: KdpA, KdpB and KdpC.
Calcium-transporting ATPase, cytoplasmic domain N
Calcium-transporting ATPase, cytoplasmic transduction domain A
POTASSIUM-TRANSPORTING ATPASE ATP-BINDING SUBUNIT
ATP phosphohydrolase [potassium-transporting] B chain
Potassium-binding and translocating subunit B
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily.
POTASSIUM-TRANSPORTING ATPASE KDPC SUBUNIT
ATP phosphohydrolase [potassium-transporting] C chain
Potassium-binding and translocating subunit C
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE
3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE, MITOCHONDRIAL
CMP-2-keto-3-deoxyoctulosonic acid synthase
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Guanylate Kinase phosphate binding domain
Essential for recycling GMP and indirectly, cGMP.
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
LOW AFFINITY POTASSIUM TRANSPORT SYSTEM PROTEIN KUP
Probable potassium transport system protein Kup
Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Belongs to the HAK/KUP transporter (TC 2.A.72) family.
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD.
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
The pilH gene encodes an ABC transporter required for type IV pilus biogenesis in Myxococcus xanthus.
PREPILIN LEADER PEPTIDASE/N-METHYLTRANSFERASE-RELATED
TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME
Prepilin leader peptidase/N-methyltransferase
Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Isocitrate/Isopropylmalate dehydrogenase-like
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.
3-isopropylmalate dehydratase large subunit
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT
3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED
Belongs to the LeuD family. LeuD type 1 subfamily.
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Leucyl/phenylalanyl-tRNA-protein transferase, C-terminal domain
Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain
LEUCYL/PHENYLALANYL-TRNA--PROTEIN TRANSFERASE
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Sequence analysis of SR171 mutant of the branched-chain keto acid dehydrogenase complex in Myxococcus xanthus.
Nucleoside Triphosphate Pyrophosphohydrolase
LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
In the N-terminal section; belongs to the LipB family.
LIPOPROTEIN-RELEASING SYSTEM ATP-BINDING PROTEIN LOLD
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
The complex is composed of two ATP-binding proteins (LolD) and two transmembrane proteins (LolC and LolE).
Belongs to the ABC transporter superfamily. Lipoprotein translocase (TC 3.A.1.125) family.
ATP DEPENDENT LON PROTEASE FAMILY MEMBER
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Homohexamer. Organized in a ring with a central cavity.
Expressed during both vegetative growth and development.
Udp N-acetylglucosamine O-acyltransferase, C-terminal domain
ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE
ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the transferase hexapeptide repeat family. LpxA subfamily.
LIPID-A-DISACCHARIDE SYNTHASE, MITOCHONDRIAL-RELATED
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED
UDP-3-O-acyl-N-acetylglucosamine deacetylase
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE
UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
TETRAACYLDISACCHARIDE 4'-KINASE, MITOCHONDRIAL-RELATED
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Transferase(Phosphotransferase) domain 1
MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED
Essential for growth. Interacts with MglA to control social gliding motility.
Belongs to the protein kinase superfamily. Tyr protein kinase family.
This lectin might have a role in the differentiation of cells.
M.xanthus is a rod-shaped bacterium with a complex life cycle that includes formation of fruiting bodies. This protein is induced during the aggregation phase of fruiting body formation.
Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))
Catalyzes the reversible oxidation of malate to oxaloacetate.
Belongs to the LDH/MDH superfamily. MDH type 3 family.
Three two-component regulatory systems of the family PhoR/PhoP control the expression of phosphatases and genes involved in energy metabolism and protein synthesis during Myxococcus xanthus development.
2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Belongs to the TPP enzyme family. MenD subfamily.
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
ligand shared between two neighboring subunits
METHIONINE IMPORT ATP-BINDING PROTEIN METN
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (MetN), two transmembrane proteins (MetI) and a solute-binding protein (MetQ).
Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.
Transcription-repair-coupling factor, D7 domain
ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
In the N-terminal section; belongs to the UvrB family.
In the C-terminal section; belongs to the helicase family. RecG subfamily.
Required for multicellular development and for both mechanisms of gliding: social (S) and adventurous (A) motility. Acts as an intracellular switch to coordinate A and S motilities. Controls the direction of gliding and gliding speed.
Belongs to the small GTPase superfamily. Arf family. MglA subfamily.
Dimethylallyl diphosphate:tRNA dimethylallyltransferase
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Methylthiotransferase, N-terminal domain
MiaB/RimO family radical SAM methylthiotransferase
CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1
MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase
(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the methylthiotransferase family. MiaB subfamily.
Cell division topological specificity factor MinE
Cell division protein MinE topological specificity domain
Cell division topological specificity factor
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Adenine nucleotide alpha hydrolases-like domains
MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1
TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
GidA associated domain, C-terminal subdomain
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Probably functions as a manganese efflux pump.
PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG
UDP-MurNAc-pentapeptide phosphotransferase
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Belongs to the glycosyltransferase 4 family. MraY subfamily.
division/cell wall cluster transcriptional repressor MraZ
LARGE-CONDUCTANCE MECHANOSENSITIVE CHANNEL
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Oxidoreductase, molybdopterin-binding domain
PROTEIN-METHIONINE-SULFOXIDE REDUCTASE CATALYTIC SUBUNIT MSRP
Oxidoreductase molybdopterin-binding domain
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ).
Is attached to the inner membrane when interacting with the MsrQ subunit.
translation initiation factor eif-2b, domain 1
S-methyl-5-thioribose-1-phosphate isomerase
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Class II aldolase/adducin N-terminal domain
METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Belongs to the aldolase class II family. MtnB subfamily.
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
1,2-DIHYDROXY-3-KETO-5-METHYLTHIOPENTENE DIOXYGENASE
Acireductone dioxygenase (Fe(2+)-requiring)
Acireductone dioxygenase (Ni(2+)-requiring)
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Belongs to the acireductone dioxygenase (ARD) family.
May play a role in metal incorporation in vivo
May play a role in transmitting local conformational changes
UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE
UDP-N-acetylglucosamine enolpyruvyl transferase
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Belongs to the EPSP synthase family. MurA subfamily.
2-(S-cysteinyl)pyruvic acid O-phosphothioketal
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
FAD-binding/transporter-associated domain-like
Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain
UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED
MurD-like peptide ligases, catalytic domain
MurD-like peptide ligases, peptide-binding domain
UDP-N-acetylmuramoyl-L-alanine synthetase
UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE 1
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Belongs to the glycosyltransferase 28 family. MurG subfamily.
MutL, C-terminal domain, dimerisation subdomain
MutL, C-terminal domain, regulatory subdomain
DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Belongs to the DNA mismatch repair MutL/HexB family.
DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER
DNA MISMATCH REPAIR PROTEIN MUTS, TYPE 2
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.
DNA MISMATCH REPAIR PROTEIN MSH1, MITOCHONDRIAL
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Belongs to the DNA mismatch repair MutS family.
nicotinate (nicotinamide) nucleotide adenylyltransferase
NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED
Probable nicotinate-nucleotide adenylyltransferase
Nicotinate mononucleotide adenylyltransferase
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Nucleoside diphosphate kinase-like domain
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
archaeoglobus fulgidus dsm 4304 superfamily
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
SODIUM ION/PROTON ANTIPORTER NHAA-RELATED
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family.
In the C-terminal section; belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family.
Belongs to the transcriptional regulatory CopG/NikR family.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
BIFUNCTIONAL DTTP/UTP PYROPHOSPHATASE/METHYLTRANSFERASE PROTEIN-RELATED
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Belongs to the Maf family. YhdE subfamily.
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
Belongs to the complex I subunit 3 family.
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex.
Belongs to the complex I 20 kDa subunit family.
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL
NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT
Belongs to the complex I 49 kDa subunit family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Belongs to the complex I subunit 1 family.
NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL
Belongs to the complex I 23 kDa subunit family.
NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L
Belongs to the complex I subunit 4L family.
Belongs to the complex I subunit 2 family.
ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN
N UTILIZATION SUBSTANCE PROTEIN B-RELATED
Transcription antitermination protein NusB
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
the outer membrane receptor (omr) family
Carboxypeptidase-like, regulatory domain
TonB-dependent receptor, beta-barrel domain
Required for secretion of the protease PopC across the bacterial outer membrane (PubMed:30911012). Binds and probably transports PopC from the periplasm to the extracellular milieu (PubMed:30911012). It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB (PubMed:30911012). Required for cellular adhesion during fruiting body formation, a multicellular developmental program that is induced in response to starvation (PubMed:8335633).
Interacts with TonB (PubMed:30911012). Part of a transport system composed of the outer membrane transporter Oar, the trans-periplasmic binding protein TonB and the inner membrane proteins ExbB and ExbD (PubMed:30911012).
The TonB box in the Oar plug domain is important for PopC secretion.
The deletion mutant is impaired in PopC secretion and does not accumulate the intercellular C-signal protein (p17) (PubMed:30911012). Disruption of the gene results in a severe defect in the development of fruiting bodies (PubMed:8335633). The deletion mutant has a growth rate similar to the wild type and displays normal type IV pili-dependent motility and gliding motility (PubMed:30911012).
Belongs to the TonB-dependent receptor family.
DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED
MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2
Obg GTP-binding protein N-terminal domain
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Aspartate/ornithine carbamoyltransferase
ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL
ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Pantoate-beta-alanine ligase, C-terminal domain
CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
The reaction proceeds by a bi uni uni bi ping pong mechanism.
Belongs to the pantothenate synthetase family.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Binds 1 pyruvoyl group covalently per subunit.
Heterooctamer of four alpha and four beta subunits.
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Schiff-base intermediate with substrate; via pyruvic acid
This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:9683657). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also carboxylates acetyl-CoA, butyryl-CoA and succinyl-CoA (PubMed:9683657).
Optimum temperature is 25-30 degrees Celsius.
Dodecamer composed of six biotin-containing alpha subunits and six beta subunits.
Consists of an N-terminal biotin carboxylation/carboxylase (BC) domain that catalyzes the transient carboxylation of the biotin covalently attached to the C-terminal biotinyl-binding/biotin carboxyl carrier (BCC) domain.
During development the activity increased gradually with the maximum during the sporulation stage.
Phosphoenolpyruvate Carboxykinase, domain 1
Phosphoenolpyruvate Carboxykinase, domain 2
PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP]
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.
PYRUVATE, PHOSPHATE DIKINASE REGULATORY PROTEIN 1, CHLOROPLASTIC
Putative pyruvate, phosphate dikinase regulatory protein
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PDRP subfamily.
Pyridoxine/pyridoxamine 5'-phosphate oxidase
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Phosphoglycerate kinase, N-terminal domain
PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED
Belongs to the phosphoglycerate kinase family.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 4-471 IN COMPLEX WITH FAD AND ACIFLUORFEN
FAD-linked reductases, C-terminal domain
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (PubMed:8621504). Does not oxidize coproporphyrinogen III (PubMed:8621504). Involved in the classical protoporphyrin-dependent (PPD) heme b biosynthesis (PubMed:28123057).
Monomer (PubMed:17046834). Homodimer (PubMed:8621504).
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.
Phosphonates import ATP-binding protein PhnC
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PhnC), two transmembrane proteins (PhnE) and a solute-binding protein (PhnD).
Belongs to the ABC transporter superfamily. Phosphonates importer (TC 3.A.1.9.1) family.
The fusion between the ATP-binding domain and LysR substrate binding domain is unusual. It could be due to a sequencing error.
Major component of the type IV pili that are required for social gliding motility through cycles of extension and retraction. Extended pili are composed of thousands of copies of PilA and retract upon binding to extracellular polysaccharides and thereby pull the cell forward.
The two-component PilS2/PilR2 is required for proper assembly of T4P and regulation.
By the two-component system PilR/PilS component PilR (PubMed:9401034). In the contrary, PilS is a negative regulator of pilA expression. In addition, an increased level of c-di-GMP correlates with reduced transcription of the pilA gene (PubMed:26124238). Expression of pilA seems to be negatively regulated by the accumulation of pilin at a cell end (PubMed:15743959, PubMed:9401034).
Deletion mutants show loss of observable pili.
Pilin assembly limits pilus production and S motility. This limitation could be linked to the high frequency of reversal of gliding direction observed in M.xanthus. Reversal implies loss of pili at the leading pole of the cell and commissioning of new pili assembly at the other pole.
Deficient in S motility despite its ability to produce surface pili.
Complete loss of detectable cell-surface PilA; when associated with N-104.
Complete loss of detectable cell-surface PilA; when associated with V-32.
Type II secretion system, protein E, N-terminal domain
TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED
ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Acts as a molecular motor to provide the energy that is required for biogenesis of the pilus and the extrusion of substrates generated in the cytoplasm (PubMed:28779124, PubMed:26965631). PilB ATPase activity is also essential for T4P extension while antagonist PilT ATPase activity is required for T4P retraction (PubMed:18223089). In addition, functions as a regulator of exopolysaccharide (EPS) downstream of the T4P filament and upstream of the Dif signaling (PubMed:28779124).
Homohexamer (By similarity). Interacts with PilC (PubMed:26851283). Interacts with PilM (PubMed:26851283).
The ATP-binding site is essential for assembly of pili.
Deletion mutants show complete loss of T4P-dependent motility since they did not assemble T4P (PubMed:18223089, PubMed:28779124). PilB and PilT double mutant also lack T4P-dependent motility (PubMed:26965631).
Restored exopolysaccharide (EPS) production of PilA mutant.
Type II secretion system (T2SS), domain F
Essential inner membrane component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (By similarity). Controls both pilus assembly and disassembly and plays an important role in PilB localization to the complex and ATPase activity (PubMed:26851283).
Homotetramer (By similarity). Interacts with PilB (PubMed:26851283).
Deletion mutant show missing type IV cytoplasmic dome and disc but the cytoplasmic ring is still present.
PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE
PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE
Protein-L-isoaspartate O-methyltransferase 1
L-isoaspartyl protein carboxyl methyltransferase 1
Protein L-isoaspartyl methyltransferase 1
Protein-beta-aspartate methyltransferase 1
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Protein-L-isoaspartate O-methyltransferase 2
L-isoaspartyl protein carboxyl methyltransferase 2
Protein L-isoaspartyl methyltransferase 2
Protein-beta-aspartate methyltransferase 2
L-isoaspartyl protein carboxyl methyltransferase
Protein-beta-aspartate methyltransferase
predicted glycosyltransferase like domains
Plays an essential role in proper timing of early development events.
May be regulated by calcium or a calmodulin-like protein.
Developmentally regulated to start immediately before spore formation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Regulates the activity of endogenous beta-lactamase or related enzymes, by blocking their secretion by phosphorylation, in response to an external signal yet to be identified.
Sequence analysis of 13 eukaryotic-like protein Ser/Thr kinases of Myxococcus xanthus, a developmental bacterium and significance of their coexistence with protein His kinases.
Pkn5 and pkn6 may have reciprocal roles in growth and development. Pkn5 may be a kinase that negatively regulates development.
Expressed constitutively throughout the life cycle, with slight increases at an early stage of development.
Pkn5 and pkn6 may have reciprocal roles in growth and development. Pkn6 may be a transmembrane sensor of external signals for development.
Autophosphorylated on serine and threonine residues.
2 X 12 AA repeats of P-[VA]-D-S-T-S-P-T-T-P-M-P
FATTY ACID/PHOSPHOLIPID SYNTHESIS PROTEIN PLSX
Acyl-[acyl-carrier-protein]--phosphate acyltransferase
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Homodimer. Probably interacts with PlsY.
Associated with the membrane possibly through PlsY.
glycerol-3-phosphate 1-O-acyltransferase PlsY
GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED
Acyl-phosphate--glycerol-3-phosphate acyltransferase
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE
POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL
Eukaryotic type KH-domain (KH-domain type I)
Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Belongs to the polyribonucleotide nucleotidyltransferase family.
P-LOOP CONTAINING NUCLEOSIDE TRIPHOSPHATE HYDROLASE
Spatial regulator of cell division that is involved in identifying the incipient division site, recruiting FtsZ to the division site and stabilizing the Z-ring. Binds ATP and GTP.
Interacts with FtsZ in pull-down experiments.
Localization is dynamic and cell cycle regulated. Accumulates at the division site at mid-cell after chromosome segregation but prior to FtsZ as well as in the absence of FtsZ.
Deletion results in division defects with the formation of filamentous cells and chromosome-free minicells. It causes reduced formation of Z-rings and incorrect positioning of the few Z-rings formed. Deletion does not affect chromosome replication and segregation (PubMed:23145985). Inactivation affects adventurous (A) gliding motility (PubMed:12828649).
Lack of activity. Cannot complement the deletion mutant.
Required for fruiting body formation, a multicellular developmental program that is induced in response to starvation (PubMed:18854146). Acts as a subtilisin-like protease that directly cleaves the CsgA precursor protein (p25) on the cell surface to generate the intercellular C-signal protein (p17) in starving cells (PubMed:18854146). Preferentially acts in cis, i.e. PopC secreted by a cell only cleaves p25 on that cell (PubMed:18854146). May also be important for processing of other protein(s) that are important for development (PubMed:18854146).
In non-starving cells, secretion and protease activity are inhibited by formation of a cytoplasmic complex with PopD (PubMed:22404381). In response to starvation, PopD is degraded in a RelA- and FtsH(D)-dependent manner, thereby releasing pre-formed PopC for secretion (PubMed:22404381). Secreted and active during starvation, and rapidly degraded upon secretion (PubMed:18854146). Secretion is significantly and reversibly reduced by carbonyl cyanide m-chlorophenyl hydrazine (CCCP), which dissipates or reduces the proton motive force (PMF), and by nigericin, which affects the pH gradient (PubMed:30911012).
Interacts with PopD in non-starving cells.
Secreted in a two-step mechanism: PopC accumulates in the periplasm before secretion to the extracellular milieu in response to starvation (PubMed:30911012). Secretion across the outer membrane depends on the transporter Oar and on the ExbB/ExbD/TonB system (PubMed:30911012). Does not contain a signal peptide and is secreted as a full-length protein (PubMed:30911012).
Disruption mutant does not show any signs of fruiting body formation even after 120 hours of starvation (PubMed:18854146). Sporulation is strongly reduced (PubMed:18854146). The precursor protein p25 accumulates as in the wild type strain, but p17 is not detected (PubMed:18854146).
Loss of activity. Cannot cleave p25. Cannot complement the developmental defects of the disruption mutant.
Inhibitor of protease PopC (PubMed:22404381). In non-starving cells, forms a cytoplasmic complex with PopC and inhibits PopC secretion and activity (PubMed:22404381).
In response to starvation, RelA is activated resulting in the accumulation of (p)ppGpp, which causes the degradation of PopD in an FtsH(D)-dependent manner, thereby releasing pre-formed PopC for secretion.
Interacts with PopC in non-starving cells.
Deletion mutant has a severe growth defect, forms tan colonies and fails to develop (PubMed:22404381). Mutant shows increased accumulation of PopC in the supernatant (PubMed:22404381).
PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Belongs to the nucleoside phosphorylase PpnP family.
ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE
Belongs to the methyltransferase superfamily. PrmA family.
DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE
Glutamyl-gamma-semialdehyde dehydrogenase
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Belongs to the glutamate 5-kinase family.
Probably a dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Involved in defense against bacteriophages (Probable). Expression of gasdermin bGSDM and this neighboring protease is toxic in E.coli (PubMed:35025633).
A late-developmental spore coat protein.
Secreted across the membrane to assemble on the spore surface.
PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL
Phosphatidylserine decarboxylase proenzyme
Phosphatidylserine decarboxylase alpha chain
Phosphatidylserine decarboxylase beta chain
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
Charge relay system; for autoendoproteolytic cleavage activity
Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity
Cleavage (non-hydrolytic); by autocatalysis
Phosphate import ATP-binding protein PstB
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS).
Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.
Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Belongs to the pseudouridine-5'-phosphate glycosidase family.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Phosphoribosylformylglycinamidine synthase, linker domain
PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE
Formylglycinamide ribonucleotide amidotransferase
Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
In the N-terminal section; belongs to the FGAMS family.
TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3
TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED
Phosphoribosylformylglycinamidine cyclo-ligase
Phosphoribosyl-aminoimidazole synthetase
BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC
BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH
Phosphoribosylaminoimidazolecarboxamide formyltransferase
The IMP cyclohydrolase activity resides in the N-terminal region.
Adenylosuccinate Synthetase, subunit A, domain 1
Adenylosuccinate Synthetase, subunit A, domain 2
Adenylosuccinate Synthetase, subunit A, domain 3
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Belongs to the adenylosuccinate synthetase family.
PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL
Formylglycinamide ribonucleotide amidotransferase subunit II
Phosphoribosylformylglycinamidine synthase subunit II
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ
Formylglycinamide ribonucleotide amidotransferase subunit I
Phosphoribosylformylglycinamidine synthase subunit I
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE
5'-phosphoribosylglycinamide transformylase 2
Non-folate glycinamide ribonucleotide transformylase
Phosphoribosylglycinamide formyltransferase 2
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL
DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Belongs to the OMP decarboxylase family. Type 1 subfamily.
Belongs to the OMP decarboxylase family. Type 2 subfamily.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.
CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.
Catalyzes the reversible phosphorylation of UMP to UDP.
S-ADENOSYLMETHIONINE:TRNA RIBOSYLTRANSFERASE-ISOMERASE
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE
Tetrahydrobiopterin biosynthesis enzymes-like
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
RIBOSOME-BINDING FACTOR A, CHLOROPLASTIC-RELATED
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes.
MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
There are two genes for RecA in M.xanthus; recA1 seems less functional than recA2.
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Recombination protein O, C-terminal domain
Involved in DNA repair and RecF pathway recombination.
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
BIFUNCTIONAL (P)PPGPP SYNTHASE/HYDROLASE SPOT
GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE
In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity).
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Belongs to the prokaryotic/mitochondrial release factor family.
Identification of serine/threonine kinase associate proteins in M. xanthus by yeast two-hybrid system.
the atp-binding cassette (abc) superfamily
CAPSULE POLYSACCHARIDE EXPORT INNER-MEMBRANE PROTEIN CTRC
O-antigen export system permease protein RfbA
May form an ATP-driven O-antigen export apparatus, in association with RfbB.
Belongs to the ABC-2 integral membrane protein family.
abc- transporter (atp binding component) like domain
TEICHOIC ACIDS EXPORT ATP-BINDING PROTEIN TAGH
O-antigen export system ATP-binding protein RfbB
May form an ATP-driven O-antigen export apparatus, in association with RfbA.
Belongs to the ABC transporter superfamily.
the putative vectorial glycosyl polymerization (vgp) family
GLYCO_TRANS_2-LIKE DOMAIN-CONTAINING PROTEIN
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
The PRC barrel domain binds ribosomal protein uS19.
30S ribosomal protein S12 methylthiotransferase RimO
RIBOSOMAL PROTEIN S12 METHYLTHIOTRANSFERASE RIMO
Ribosomal protein uS12 methylthiotransferase RimO
Ribosomal protein uS12 (aspartate-C(3))-methylthiotransferase
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Belongs to the methylthiotransferase family. RimO subfamily.
Ribosome maturation factor RimP, C-terminal domain
Required for maturation of 30S ribosomal subunits.
6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the universal ribosomal protein uL10 family.
Ribosomal protein L11, C-terminal domain
Ribosomal protein L11/L12, N-terminal domain
39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
One or more lysine residues are methylated.
Belongs to the universal ribosomal protein uL11 family.
54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8.
Belongs to the universal ribosomal protein uL14 family.
39S RIBOSOMAL PROTEIN L15, MITOCHONDRIAL
Belongs to the universal ribosomal protein uL15 family.
39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Belongs to the universal ribosomal protein uL16 family.
39S RIBOSOMAL PROTEIN L17, MITOCHONDRIAL
Part of the 50S ribosomal subunit. Contacts protein L32.
Belongs to the bacterial ribosomal protein bL17 family.
39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
Belongs to the universal ribosomal protein uL18 family.
39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Belongs to the bacterial ribosomal protein bL19 family.
Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Belongs to the universal ribosomal protein uL1 family.
50S RIBOSOMAL PROTEIN L20, CHLOROPLASTIC
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Belongs to the bacterial ribosomal protein bL20 family.
39S RIBOSOMAL PROTEIN L21, MITOCHONDRIAL
This protein binds to 23S rRNA in the presence of protein L20.
Part of the 50S ribosomal subunit. Contacts protein L20.
Belongs to the bacterial ribosomal protein bL21 family.
50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC
CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Belongs to the universal ribosomal protein uL22 family.
RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome.
Belongs to the universal ribosomal protein uL23 family.
39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Belongs to the universal ribosomal protein uL24 family.
RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18.
Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the bacterial ribosomal protein bL28 family.
Belongs to the universal ribosomal protein uL29 family.
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the universal ribosomal protein uL2 family.
Ribosomal protein L30, ferredoxin-like fold domain
39S RIBOSOMAL PROTEIN L30, MITOCHONDRIAL
Belongs to the universal ribosomal protein uL30 family.
50S RIBOSOMAL PROTEIN L31, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Belongs to the bacterial ribosomal protein bL32 family.
50S RIBOSOMAL PROTEIN L33, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL33 family.
54S RIBOSOMAL PROTEIN L39, MITOCHONDRIAL
39S RIBOSOMAL PROTEIN L34, MITOCHONDRIAL
MITOCHONDRIAL RIBOSOMAL PROTEIN 34 FAMILY MEMBER
Belongs to the bacterial ribosomal protein bL34 family.
Belongs to the bacterial ribosomal protein bL35 family.
50S RIBOSOMAL PROTEIN L36, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL36 family.
50S RIBOSOMAL PROTEIN L3-1, CHLOROPLASTIC
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.
Belongs to the universal ribosomal protein uL3 family.
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Forms part of the polypeptide exit tunnel.
Belongs to the universal ribosomal protein uL4 family.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the universal ribosomal protein uL5 family.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Belongs to the universal ribosomal protein uL6 family.
39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL
Ribosomal protein L7/12, oligomerisation (N-terminal) domain
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
Belongs to the bacterial ribosomal protein bL12 family.
Belongs to the bacterial ribosomal protein bL9 family.
PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3
Ribosomal RNA large subunit methyltransferase E
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE H
23S rRNA (pseudouridine1915-N3)-methyltransferase
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Belongs to the RNA methyltransferase RlmH family.
Dual-specificity RNA methyltransferase RlmN 1
23S rRNA (adenine(2503)-C(2))-methyltransferase 1
Ribosomal RNA large subunit methyltransferase N 1
tRNA (adenine(37)-C(2))-methyltransferase 1
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Belongs to the radical SAM superfamily. RlmN family.
Dual-specificity RNA methyltransferase RlmN 2
23S rRNA (adenine(2503)-C(2))-methyltransferase 2
Ribosomal RNA large subunit methyltransferase N 2
tRNA (adenine(37)-C(2))-methyltransferase 2
Dual-specificity RNA methyltransferase RlmN
23S rRNA (adenine(2503)-C(2))-methyltransferase
Ribosomal RNA large subunit methyltransferase N
tRNA (adenine(37)-C(2))-methyltransferase
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Ribonuclease H-like superfamily/Ribonuclease H
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Homohexameric ring arranged as a trimer of dimers.
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
DNA-directed RNA polymerase, insert domain
C-terminal domain of RNA polymerase alpha subunit
Insert subdomain of RNA polymerase alpha subunit
DNA-directed RNA polymerase subunit alpha
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Belongs to the RNA polymerase alpha chain family.
DNA-directed RNA polymerase, beta subunit, external 1 domain
DNA-directed RNA polymerase, subunit 2, domain 6
RNA polymerase alpha subunit dimerisation domain
DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA
beta and beta-prime subunits of DNA dependent RNA-polymerase
The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Belongs to the RNA polymerase beta chain family.
DNA-directed RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (By similarity). Also required for extracellular A-signal production. The A-signal is the first in a series of extracellular signals that are required for myxspore differentiation in M.xanthus. It is thought to act as a cell-density signal during early development to ensure there are enough cells present to complete fruiting-body morphogenesis. A variant at residue 598 prevents A-signal production in an unknown fashion.
Interacts transiently with the RNA polymerase catalytic core.
Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
Interaction with polymerase core subunit RpoC
In allele asgC767; unable to produce the A-signal, otherwise growth is unaffected.
DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Belongs to the RNA polymerase subunit omega family.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is essential for late-stage differentiation of M.xanthus.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is essential for normal fruiting body formation.
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to IF-3.
Belongs to the universal ribosomal protein uS11 family.
28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL
With S4 and S5 plays an important role in translational accuracy.
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.
Belongs to the universal ribosomal protein uS12 family.
Identification of a histidine kinase (KfaA) for FruA of Myxococcus xanthus.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Belongs to the universal ribosomal protein uS13 family.
28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
Belongs to the universal ribosomal protein uS14 family.
37S RIBOSOMAL PROTEIN S28, MITOCHONDRIAL
RIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.
Belongs to the universal ribosomal protein uS15 family.
28S RIBOSOMAL PROTEIN S16, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bS16 family.
37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS17 family.
28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6.
Belongs to the bacterial ribosomal protein bS18 family.
37S RIBOSOMAL PROTEIN S19, MITOCHONDRIAL
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
30S RIBOSOMAL PROTEIN S20, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bS20 family.
Belongs to the bacterial ribosomal protein bS21 family.
30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR
Belongs to the universal ribosomal protein uS2 family.
Prokaryotic type KH domain (KH-domain type II)
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.
Belongs to the universal ribosomal protein uS3 family.
37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
With S5 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Belongs to the universal ribosomal protein uS4 family.
With S4 and S12 plays an important role in translational accuracy.
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Part of the 30S ribosomal subunit. Contacts proteins S4 and S8.
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Belongs to the universal ribosomal protein uS5 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
Part of the 30S ribosomal subunit. Contacts proteins S9 and S11.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S5 and S12.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the universal ribosomal protein uS9 family.
Ribosomal RNA adenine dimethylase-like, domain 2
Ribosomal RNA small subunit methyltransferase A
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN
Ribosomal RNA small subunit methyltransferase G
16S rRNA 7-methylguanosine methyltransferase
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.
Putative methyltransferase TM0872, insert domain
16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH
12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE
Ribosomal RNA small subunit methyltransferase H
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Belongs to the methyltransferase superfamily. RsmH family.
NUCLEAR INTRON MATURASE 1, MITOCHONDRIAL-RELATED
RNA-directed DNA polymerase from retron Mx162
Reverse transcriptase (RT) responsible for synthesis of msDNA-Mx162 (a branched molecule with RNA linked by a 2',5'-phosphodiester bond to ssDNA). The retron transcript serves as primer (from a conserved internal G residue) and template for the reaction, and codes for the RT (Probable). The retron is involved in antiviral defense (By similarity).
msDNA synthesis is inhibited by rifampicin and chloramphenicol.
No production of msDNA. No other visible effect on growth, morphogenesis, fruiting body formation, spore germination or cell motility.
M.xanthus contains two independent and unlinked retrons: Mx65 and Mx162.
Retrons may be the ancestors of retrovirus.
Belongs to the bacterial reverse transcriptase family.
RNA-directed DNA polymerase from retron Mx65
Reverse transcriptase (RT) responsible for synthesis of msDNA-Mx65 (a branched molecule with RNA linked by a 2',5'-phosphodiester bond to ssDNA). The retron transcript serves as primer (from a conserved internal G residue) and template for the reaction, and codes for the RT (By similarity). The retron is involved in antiviral defense (By similarity).
Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen atoms in the process to yield ureidoacrylate peracid, that immediately reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN-N(5)-oxide reacts spontaneously with NADH to produce FMN. Requires the flavin reductase RutF to regenerate FMN in vivo.
Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA subfamily.
ISOCHORISMATASE DOMAIN-CONTAINING PROTEIN
PEROXYUREIDOACRYLATE/UREIDOACRYLATE AMIDOHYDROLASE-RELATED
Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
Belongs to the isochorismatase family. RutB subfamily.
Involved in pyrimidine catabolism. Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously. RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions.
Holliday junction branch migration complex subunit RuvA
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE RUVB
Holliday junction branch migration complex subunit RuvB
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE RUVC
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Homodimer which binds Holliday junction (HJ) DNA. The HJ becomes 2-fold symmetrical on binding to RuvC with unstacked arms; it has a different conformation from HJ DNA in complex with RuvA. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
Formate/glycerate dehydrogenase catalytic domain-like
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the adenosylhomocysteinase family.
In the N-terminal section; belongs to the APS kinase family.
In the C-terminal section; belongs to the sulfate adenylyltransferase family.
Helical scaffold and wing domains of SecA
SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.
Multidrug efflux transporter AcrB transmembrane domain
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Forms a complex with SecF. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.
Belongs to the SecD/SecF family. SecD subfamily.
INACTIVE SELENIDE, WATER DIKINASE-LIKE PROTEIN-RELATED
Synthesizes selenophosphate from selenide and ATP.
Belongs to the selenophosphate synthase 1 family. Class I subfamily.
PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Phosphohydroxythreonine aminotransferase
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
May stabilize cellular components during stress and spore formation.
During fruiting and upon induced sporulation.
By stress, such as heat shock and oxygen limitation.
Belongs to the small heat shock protein (HSP20) family.
TMRNA-BINDING COMPONENT OF TRANS-TRANSLATION TAGGING COMPLEX
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
The tmRNA-SmpB complex associates with stalled 70S ribosomes.
FMNH2-dependent aliphatic sulfonate monooxygenase
Catalyzes the desulfonation of aliphatic sulfonates.
SUCCINATE--COA LIGASE [GDP-FORMING] SUBUNIT BETA, MITOCHONDRIAL
Succinate--CoA ligase [ADP-forming] subunit beta
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Heterotetramer of two alpha and two beta subunits.
Belongs to the succinate/malate CoA ligase beta subunit family.
Survival protein SurE-like phosphatase/nucleotidase
Nucleoside 5'-monophosphate phosphohydrolase
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Binds 1 divalent metal cation per subunit.
Belongs to the SurE nucleotidase family.
Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS)
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Cysteine-tRNA ligase, C-terminal anti-codon recognition domain
Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
Belongs to the class-I aminoacyl-tRNA synthetase family.
Non-discriminating aspartyl-tRNA synthetase
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Glutamate-tRNA synthetase, class I, anticodon-binding domain 1
GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED
An anticodon-binding domain of class I aminoacyl-tRNA synthetases
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL
Phenylalanine--tRNA ligase alpha subunit
Phenylalanyl-tRNA synthetase alpha subunit
Tetramer of two alpha and two beta subunits.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
Ferrodoxin-fold anticodon-binding domain
Phenylalanyl-trna Synthetase, Chain B, domain 3
PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47
Phenylalanyl-tRNA synthetase beta subunit
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
GLYCINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2
LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL
LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
Methionyl-tRNA synthetase (MetRS), Zn-domain
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.
ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
YbaK/aminoacyl-tRNA synthetase-associated domain
MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
BIFUNCTIONAL GLUTAMATE/PROLINE--TRNA LIGASE
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.
Arginyl tRNA synthetase N-terminal domain
Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Homodimer. The tRNA molecule binds across the dimer.
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
THREONINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Belongs to the tryptophan 2,3-dioxygenase family.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the transaldolase family. Type 3B subfamily.
Has aminomutase and, to a lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine, which is incorporated into secondary metabolites called chondramides. The aminomutase activity mainly produces R-beta-tyrosine but also S-beta tyrosine in smaller amounts. Does not accept D-tyrosine, L-histidine or L-phenylalanine as substrates.
377 uM for L-tyrosine (tyrosine 2,3-aminomutase activity)
Loss of aminomutase activity and increased product racemization. Gain of ammonia-lyase activity.
Loss of aminomutase and ammonia-lyase activity. Higher enantiomeric excess of (R)-beta-tyrosine.
Loss of aminomutase and ammonia-lyase activity.
Has aminomutase and, to a much lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to S-beta-tyrosine, which is probably incorporated into secondary metabolite myxovalargin. The aminomutase activity exclusively produces S-beta-tyrosine.
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon.
Medium-chain alcohol dehydrogenases, catalytic domain
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Belongs to the zinc-containing alcohol dehydrogenase family.
Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.
Belongs to the queuine tRNA-ribosyltransferase family.
RNA binding; important for wobble base 34 recognition
Involved in the incorporation of a chlorinated tryptophan residue into halogenated forms of the secondary metabolites called chondramides.
Belongs to the flavin-dependent halogenase family.
PHOSPHOMETHYLPYRIMIDINE SYNTHASE, CHLOROPLASTIC
Hydroxymethylpyrimidine phosphate synthase
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Belongs to the thiamine-phosphate synthase family.
THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Homotetramer. Forms heterodimers with either ThiH or ThiS.
TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE
TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC
Triger factor/SurA peptide-binding domain-like
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Belongs to the FKBP-type PPIase family. Tig subfamily.
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the triosephosphate isomerase family.
tRNA (guanosine(46)-N7)-methyltransferase TrmB
3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE
tRNA (guanine(46)-N(7))-methyltransferase
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Specifically methylates guanosine-37 in various tRNAs.
Belongs to the RNA methyltransferase TrmD family.
METHYLENETETRAHYDROFOLATE--TRNA-(URACIL-5-)-METHYLTRANSFERASE TRMFO
Folate-dependent tRNA (uracil-5-)-methyltransferase
Folate-dependent tRNA(M-5-U54)-methyltransferase
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Belongs to the MnmG family. TrmFO subfamily.
Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Belongs to the anthranilate phosphoribosyltransferase family.
N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE
Pseudouridine synthase I, catalytic domain, C-terminal subdomain
Pseudouridine synthase I, catalytic domain, N-terminal subdomain
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Belongs to the tRNA pseudouridine synthase TruA family.
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Belongs to the pseudouridine synthase TruD family.
TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE
TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL-RELATED
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
tRNA 2-thiocytidine biosynthesis protein TtcA
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster.
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
Carboxylation allows a single lysine to coordinate two nickel ions.
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Homodimer. UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Interacts with UvrB in an incision complex.
Divalent-metal-dependent TIM barrel enzymes
Catalyzes the dehydration of D-mannonate.
Belongs to the mannonate dehydratase family.
V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit.
ATP-SYNT_AB DOMAIN-CONTAINING PROTEIN-RELATED
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
Belongs to the V-ATPase D subunit family.
Belongs to the V-ATPase E subunit family.
lambda integrase-like, N-terminal domain
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD.
Belongs to the 'phage' integrase family. XerC subfamily.
O-(3'-phospho-DNA)-tyrosine intermediate
UPF0173 METAL-DEPENDENT HYDROLASE MJ1163-RELATED
UPF0173 METAL-DEPENDENT HYDROLASE TM_1162
UPF0173 metal-dependent hydrolase Adeh_1068
UPF0173 metal-dependent hydrolase AnaeK_1127
UPF0173 metal-dependent hydrolase A2cp1_1196
UPF0173 metal-dependent hydrolase MXAN_1394
YebC/PmpR family DNA-binding transcriptional regulator
TRANSCRIPTIONAL REGULATORY PROTEIN YEBC-RELATED
Probable transcriptional regulatory protein AnaeK_1694
Probable transcriptional regulatory protein A2cp1_1765
Nucleoid-associated protein YbaB-like domain
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Probable transcriptional regulatory protein Adeh_2184
PHOSPHORYLATION AT ASP-52 AND ASP-169 BY GCHK
RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN
Response regulator receiver protein Anae109_2439
Member of the two-component regulatory system GcHK/Anae109_2439. Is involved in a signal transduction system responding to oxygen availability.
Is monophosphorylated by GcHK, but not diphosphorylated. Is not phosphorylated at all; when associated with A-169.
Is monophosphorylated by GcHK, but not diphosphorylated. Is not phosphorylated at all; when associated with A-52.
MEMBRANE BOUND PREDICTED REDOX MODULATOR
THYLAKOID MEMBRANE PROTEIN TERC, CHLOROPLASTIC
Uncharacterized membrane protein STKORF319
Nucleoid-associated protein Anae109_3761
Probable RNA methyltransferase Adeh_4229
Transcriptional regulatory protein pf0864 domain like
nickel pincer cofactor biosynthesis protein LarC
PYRIDINIUM-3,5-BISTHIOCARBOXYLIC ACID MONONUCLEOTIDE NICKEL INSERTION PROTEIN
Probable RNA methyltransferase Anae109_4379
Multidrug resistance efflux transporter EmrE
Probable transcriptional regulatory protein MXAN_4974
DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B
SHORT CHAIN DEHYDROGENASE FAMILY PROTEIN
Uncharacterized oxidoreductase MXAN_5909
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Probable RNA methyltransferase MXAN_6459
Probable transcriptional regulatory protein MXAN_7062
Metalloproteases ('zincins'), catalytic domain
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Belongs to the endoribonuclease YbeY family.
Uncharacterized 18.1 kDa protein in carS 3'region
CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX18, MITOCHONDRIAL
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Interacts with the Sec translocase complex via SecD. Specifically interacts with transmembrane segments of nascent integral membrane proteins during membrane integration.
Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
membrane protein insertion efficiency factor YidD
MEMBRANE PROTEIN INSERTION EFFICIENCY FACTOR-RELATED
Putative membrane protein insertion efficiency factor
Could be involved in insertion of integral membrane proteins into the membrane.
POLYNUCLEOTIDYL TRANSFERASE, RIBONUCLEASE H-LIKE SUPERFAMILY PROTEIN
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.