NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
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).
Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.
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.
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Leucine Aminopeptidase, subunit E, domain 1
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Belongs to the anhydro-N-acetylmuramic acid kinase family.
N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED
N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
N-acetyl-gamma-glutamyl-phosphate reductase
N-acetyl-glutamate semialdehyde dehydrogenase
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Belongs to the NAGSA dehydrogenase family. Type 1 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.
Dehydroquinate synthase-like - alpha domain
3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
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.
ARSENIC RESISTANCE PROTEIN ARSH (AFU_ORTHOLOGUE AFUA_5G15030)
Arsenical resistance operon protein ArsH
Has NADPH-dependent FMN reductase activity and high NADPH-dependent ferric reductase activity with highest activity for Fe(3+) as substrate. No activity with NADH, iron trichloride, Cu(2+) or Ag(+). May be involved in cytosolic ferric iron assimilation as an NADPH-dependent ferric reductase in vivo.
Optimum pH is 6.5 for the ferric reductase activity.
Optimum temperature is 35 degrees Celsius for the ferric reductase activity.
Loss of ferric reductase activity. Does not bind FMN cofactor.
Strongly reduced ferric reductase activity. Binds FMN cofactor.
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.
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.
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.
ATP synthase delta/epsilon subunit, C-terminal domain
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
Epsilon subunit of F1F0-ATP synthase C-terminal domain
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.
F1F0 ATP synthase subunit B, membrane domain
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 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.
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
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.
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.
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
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.
Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows A.thiooxidans S1p to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).
kcat is 780 sec(-1) with carbon disulfide as substrate. kcat is 814 sec(-1) with the intermediate carbonyl sulfide as substrate.
32 nmol/min/ug enzyme towards hydrogen sulfide formation from carbon disulfide
34 nmol/min/ug enzyme towards hydrogen sulfide formation from carbonyl sulfide
Belongs to the beta-class carbonic anhydrase family.
Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows A.thiooxidans G8 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).
kcat is 3000 sec(-1) with carbon disulfide as substrate. kcat is 22400 sec(-1) with the intermediate carbonyl sulfide as substrate.
131 nmol/min/ug enzyme towards hydrogen sulfide formation from carbon disulfide
97 nmol/min/ug enzyme towards hydrogen sulfide formation from carbonyl sulfide
Exists as both octamers and hexadecamers in solution. The hexadecameric homooligomer may form a catenane, through interactions of two interlocked octameric rings.
CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP
Binds 2 heme c groups covalently per subunit.
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
Part of an energy-coupled inorganic carbon pump.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.
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.
Bacterial exopeptidase dimerisation domain
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Belongs to the peptidase M20A family. DapE subfamily.
Catalyzes the deamination of dCTP to dUTP.
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.
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
Belongs to the heat shock protein 70 family.
By stress conditions e.g. heat shock (By similarity).
5' to 3' exonuclease, C-terminal subdomain
CHROMOSOME TRANSMISSION FIDELITY FACTOR 18
DNA ligase/mRNA capping enzyme, catalytic domain
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.
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).
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.
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-33 is required for alleviation.
May be beta-lysylated on the epsilon-amino group of Lys-33 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC (if this protein is present). Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety may extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. Hydroxylation of the C5 position on Lys-33 may allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA.
Belongs to the elongation factor P family.
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
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.
Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation.
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.
iron-sulfur cluster assembly accessory protein
IRON-SULFUR CLUSTER ASSEMBLY 2 HOMOLOG, MITOCHONDRIAL
Iron-sulfur cluster insertion protein ErpA
Required for insertion of 4Fe-4S clusters for at least IspG.
Binds 1 iron-sulfur cluster per subunit.
Fructose-1,6-Bisphosphatase, subunit A, domain 1
SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
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.
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.
Leucine Dehydrogenase, chain A, domain 1
C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC
C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED
Aminoacid dehydrogenase-like, N-terminal domain
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.
N-terminal domain of MutM-like DNA repair proteins
DNA-(apurinic or apyrimidinic site) lyase MutM
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Proton donor; for beta-elimination activity
Proton donor; for delta-elimination activity
Glu-tRNAGln amidotransferase C subunit, N-terminal domain
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
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).
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING
GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING)
N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
L-glutamine--D-fructose-6-phosphate amidotransferase
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
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.
Glutamine synthetase/guanido kinase, catalytic domain
Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
The activity of this enzyme could be controlled by adenylation under conditions of abundant glutamine.
Oligomer of 12 subunits arranged in the form of two hexameric ring.
Belongs to the glutamine synthetase family.
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.
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.
The order of the peptides shown is uncertain. It is also unknown if gaps exist between the peptides.
NADH:ubiquinone oxidoreductase-like, 20kDa subunit
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
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.
HIGH FREQUENCY LYSOGENIZATION PROTEIN HFLD
High frequency lysogenization protein HflD homolog
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.
Ribosome hibernation promotion factor-like
Ribosome binding protein Y (YfiA homologue)
Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.
Associates exclusively with 100S ribosomes, which are dimers of 70S ribosomes.
Belongs to the HPF/YfiA ribosome-associated protein family. Long HPF subfamily.
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
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.
Heat shock protein 90, C-terminal domain
Histidine kinase-like ATPase, C-terminal domain
ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Molecular chaperone. Has ATPase activity.
Belongs to the heat shock protein 90 family.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
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.
Catalyzes the oxidation of Fe(2+) to Fe(3+) coupled to cytochrome c552 reduction.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Belongs to the high-potential iron-sulfur protein (HiPIP) family.
2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
4-diphosphocytidyl-2C-methyl-D-erythritol synthase
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Positions MEP for the nucleophilic attack
4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE
4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE (FERREDOXIN), CHLOROPLASTIC
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin)
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
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.
2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED
PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE
2-dehydro-3-deoxyphosphooctonate aldolase
3-deoxy-D-manno-octulosonic acid 8-phosphate synthase
Phospho-2-dehydro-3-deoxyoctonate aldolase
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.
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.
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.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS
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. Can also use D-malate and L-malate, with lower efficiency.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
The presence of K(+) or NH4(+) is essential for activity.
Optimum temperature is 60 degrees Celsius.
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.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
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.
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.
CONSERVED COMPONENT OF ABC TRANSPORTER FOR NATURAL AMINO ACIDS-RELATED
LIPOPOLYSACCHARIDE EXPORT SYSTEM ATP-BINDING PROTEIN LPTB
Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Component of the lipopolysaccharide transport and assembly complex. The LptBFG transporter is composed of two ATP-binding proteins (LptB) and two transmembrane proteins (LptF and LptG) (By similarity).
Belongs to the ABC transporter superfamily. Outer membrane lipopolysaccharide export (TC 1.B.42) family.
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.
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).
SEQUENCE REVISION TO 92; 440; 454-455 AND 483
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9
FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
The active site is a redox-active disulfide bond.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
MUTAGENESIS OF CYS-23; CYS-26; HIS-72; HIS-97; HIS-98; CYS-132 AND CYS-137
Inhibited by the thiol-modifying reagent N-ethylmaleimide (NEM).
REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR
Mercuric resistance operon regulatory protein
Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site.
It is not sure if the metal-binding site is on position 81 or 82.
5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Belongs to the vitamin-B12 independent methionine synthase family.
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
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Belongs to the AB hydrolase superfamily. MetX family.
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
Adenine nucleotide alpha hydrolases-like
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
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.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
This protein is essential to promote the specific transfer of the plasmid in the presence of conjugative plasmids.
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
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-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-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE 1
UDP-Glycosyltransferase/glycogen phosphorylase
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.
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).
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
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.
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.
Nitrogenase molybdenum iron protein domain
NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN
This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
Binds 1 [8Fe-7S] cluster per heterodimer.
Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
Tetramer of two alpha and two beta chains. Forms complex with the iron protein (nitrogenase component 2).
Belongs to the NifD/NifK/NifE/NifN family.
LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
The reversible ADP-ribosylation of Arg-103 inactivates the nitrogenase reductase and regulates nitrogenase activity.
ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase
Nitrogenase Molybdenum-iron Protein, subunit B, domain 4
LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B
Nitrogenase molybdenum-iron protein beta chain
Nitrogenase-stabilizing/protective protein NifW
May protect the nitrogenase Fe-Mo protein from oxidative damage.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
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:ubiquinone oxidoreductase, 30kDa subunit
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL
NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3
Belongs to the complex I 30 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.
NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L
Belongs to the complex I subunit 4L family.
Belongs to the complex I subunit 2 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.
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.
4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE
4-(phosphohydroxy)-L-threonine dehydrogenase
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
The active site is located at the dimer interface.
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Phosphoglycerate kinase, N-terminal domain
PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED
Belongs to the phosphoglycerate kinase family.
POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE
POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL
Eukaryotic type KH-domain (KH-domain type I)
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Belongs to the polyribonucleotide nucleotidyltransferase family.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Phosphoribosylaminoimidazole-succinocarboxamide synthase
Belongs to the SAICAR synthetase family.
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.
Aspartate/ornithine carbamoyltransferase
ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
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 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.
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).
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.
RuBisCO operon transcriptional regulator
Trans-acting transcriptional regulator of RuBisCO genes (rbcL1S1) expression.
Belongs to the LysR transcriptional regulatory family.
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.
Ribulose bisphosphate carboxylase, large subunit, C-terminal domain
RuBisCO large subunit, N-terminal domain
RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
RuBisCO, large subunit, small (N-terminal) domain
Ribulose bisphosphate carboxylase large chain 1
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
Heterohexadecamer of 8 large chains and 8 small chains.
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.
Belongs to the RuBisCO large chain family. Type I subfamily.
In A.ferrooxidans two similar set of genes code for RuBisCO large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23
In T.ferrooxidans two similar set of genes code for RuBisCO large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets.
Thiobacillus ferrooxidans ATCC 23270, the type strain, possesses two sets of form I ribulose bisphosphate carboxylase/oxygenase (RuBisCO) genes and a form II RuBisCO gene.
Ribulose bisphosphate carboxylase large chain 2
Ribulose bisphosphate carboxylase, small subunit
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC
Ribulose bisphosphate carboxylase small subunit 1
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Heterohexadecamer of 8 large and 8 small subunits.
Belongs to the RuBisCO small chain family.
Ribulose bisphosphate carboxylase small subunit 2
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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-346
ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Belongs to the helicase family. RecG subfamily.
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.
Functions as a primase with respect to replication at the (vegetative) origin of replication of pTF-FC2.
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Belongs to the prokaryotic/mitochondrial release factor family.
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.
Homohexamer. The homohexamer assembles into an open ring structure (By similarity).
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.
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers.
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.
39S RIBOSOMAL PROTEIN L13, MITOCHONDRIAL
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Belongs to the universal ribosomal protein uL13 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.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bL27 family.
39S RIBOSOMAL PROTEIN L28, MITOCHONDRIAL
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.
54S RIBOSOMAL PROTEIN L39, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bL33 family.
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 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.
TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE
S-adenosyl-L-methionine-dependent methyltransferases
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD
Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily.
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.
Ribonuclease H-like superfamily/Ribonuclease H
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Belongs to the RNR ribonuclease family. RNase R subfamily.
RNA polymerase sigma-54 factor, core-binding domain
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of the nitrogen fixation genes. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for receipt of the melting signal from the remotely bound activator protein NifA for the expression of the nitrogen fixation proteins.
D-ribose-5-phosphate isomerase (RpiA), lid domain
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Belongs to the ribose 5-phosphate isomerase 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
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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 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.
Nucleoside Triphosphate Pyrophosphohydrolase
DIHYDRONEOPTERIN TRIPHOSPHATE DIPHOSPHATASE
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
Belongs to the Nudix hydrolase family. RppH subfamily.
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 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.
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.
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.
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.
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.
Binds together with bS18 to 16S ribosomal RNA.
Belongs to the bacterial ribosomal protein bS6 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.
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.
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.
Electron carrier from cytochrome c552 to the A-type oxidase.
The two different versions of rusticyanins are most probably due to strain variations.
Expressed during growth on Fe(2+), sulfur and thiosulfate.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-187
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.
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.
One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.
Homotetramer, a dimer of dimers. One homotetramer interacts with 1 SecA dimer.
Phosphohydroxythreonine aminotransferase
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Binds 1 pyridoxal phosphate per subunit.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
SUGAR FERMENTATION STIMULATION PROTEIN A
Sugar fermentation stimulation protein homolog
S-adenosylmethionine decarboxylase domain
S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME
S-adenosylmethionine decarboxylase beta chain
S-adenosylmethionine decarboxylase alpha chain
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Binds 1 pyruvoyl group covalently per subunit.
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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 group blocking the N-terminus of the alpha chain.
Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Schiff-base intermediate with substrate; via pyruvic acid
Proton acceptor; for processing activity
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FAD; UBIQUINONE AND HYDROGEN SULFIDE
MUTAGENESIS OF CYS-128; CYS-160 AND CYS-356
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-434 IN COMPLEX WITH FAD; UBIQUINONE AND HYDROGEN SULFIDE
MUTAGENESIS OF SER-126; CYS-128; HIS-132; CYS-160; HIS-198 AND CYS-356
Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
No effect on FAD reduction. Strongly reduced activity with decylubiquinone.
No effect on FAD reduction. Abolishes activity with decylubiquinone.
No effect on FAD reduction. Reduced activity with decylubiquinone.
Strongly reduces FAD reduction. Abolishes activity with decylubiquinone.
Complete loss of enzyme activity. Abolishes enzyme FAD reduction. Abolishes activity with decylubiquinone.
SUCCINATE--COA LIGASE [GDP-FORMING] SUBUNIT BETA, MITOCHONDRIAL
Glutathione synthetase ATP-binding domain-like
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.
Catalyzes the reversible conversion of sucrose and a nucleotide disphosphate (NDP) into fructose and NDP-glucose; although the reaction is freely reversible in vitro, the physiological reaction seems to be sucrose cleavage. Unlike characterized plant enzymes prefers ADP as a cosubstrate, whereas plants prefer UDP. The KM for sucrose is 45-fold lower in the presence of ADP than UDP. Its preference for ADP over UDP suggests it may directly link sucrose and glycogen metabolism (Probable).
Optimum temperature is 60 degrees Celsius. Remains stable after 15 minutes at 60 degrees Celsius.
Could be used to synthesize NDP-sugars for large-scale glycosylation processes; its comparatively high thermostability would be useful.
Belongs to the glycosyltransferase 1 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.
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 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.
GLYCINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2
Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
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.
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.
Arginyl tRNA synthetase N-terminal domain
Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain
Belongs to the class-I aminoacyl-tRNA synthetase family.
Serine-tRNA synthetase, tRNA binding 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).
MUTAGENESIS OF HIS-53; HIS-306; SER-356 AND LYS-395
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 2 subfamily.
Does not complement the tyrS mutation in E.coli.
Does not complement the tyrS mutation in E.coli. 3-fold decrease in kcat for amino acid activation, without effect on Km for tyrosine or ATP.
Does not complement the tyrS mutation in E.coli. 7-fold increase in Km for E.coli tRNA, without effect on other kinetic parameters.
Complements the tyrS mutation in E.coli very poorly. 17-fold increase in Km for E.coli tRNA, without effect on Km for ATP or tyrosine.
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
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.
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.
Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the triosephosphate isomerase family.
TRANSPOSASE FOR INSERTION SEQUENCE ELEMENT IS1081
Transposase for insertion sequence element IST2
Required for the transposition of the insertion element.
Belongs to the transposase mutator 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.
TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Tetramer of two alpha and two beta chains.
Tryptophan synthase beta subunit-like PLP-dependent enzymes
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
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
YVTN repeat-like/Quinoprotein amine dehydrogenase
OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMB
Catalyzes the hydrolysis of tetrathionate to generate elemental sulfur, thiosulfate and sulfate.
Belongs to the tetrathionate hydrolase family.
No change in activity. Does not affect dimerization.
YebC/PmpR family DNA-binding transcriptional regulator
TRANSCRIPTIONAL REGULATORY PROTEIN YEBC-RELATED
Probable transcriptional regulatory protein AFE_0059
Probable transcriptional regulatory protein Lferr_0060
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.
UPF0194 membrane protein in asrC 5'region
Comparisons with its orthologs suggests that this protein may be full-length.
INTRACELLULAR SEPTATION PROTEIN A-RELATED
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Uncharacterized 18.9 kDa protein in mobE 3'region
Uncharacterized 5.9 kDa protein in mobE 3'region
Uncharacterized 9.0 kDa protein in mobE 3'region
Uncharacterized 8.2 kDa protein in mobL 3'region
Uncharacterized 12.3 kDa protein in mobL 3'region
Uncharacterized 15.6 kDa protein in mobL 3'region
Uncharacterized 11.6 kDa protein in mobS 3'region