P-loop containing nucleotide triphosphate hydrolases
ABC TRANSPORTER I FAMILY MEMBER 6, CHLOROPLASTIC
P-loop containing nucleoside triphosphate hydrolases
Probable ATP-dependent transporter ycf16
Belongs to the ABC transporter superfamily. Ycf16 family.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
Whole genome sequence of Porphyra yezoensis chloroplast.
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-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.
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Belongs to the aconitase/IPM isomerase 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.
MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER [OXIDATIVE] CYCLASE, CHLOROPLASTIC
Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase
Mg-protoporphyrin IX monomethyl ester oxidative cyclase
Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME).
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
PHYCOBILISOME 32.1 KDA LINKER POLYPEPTIDE, PHYCOCYANIN-ASSOCIATED, ROD 2-RELATED
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
Heterodimer of an alpha and a beta chain.
Contains one covalently linked phycocyanobilin chromophore.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-161
Although originally identified as Cyanidium caldarium, these sequences derive from Galdieria sulphuraria.
Cloning and sequence analysis of allophycocyanin gene of Porphyra haitanensis.
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers (By similarity).
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH APCA AND PHYCOCYANOBILIN
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
Heterododecamer of 6 alpha and 6 beta chains. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer.
The light-harvesting antenna system in red algae and cyanobacteria is formed of phycobilisomes. These are composed of the phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin (PCC). The phycobiliproteins all share the same subunit composition and organization with variations in the covalently bound open-chain tetrapyrrole chromophores. The phycobiliprotein complexes are arranged sequentially in antenna complexes linked by linker proteins with CPE at the periphery, CPC in the middle and APC at the core feeding to the photosynthetic reaction center. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
Neither a protein sequence nor a nucleotide sequence has been determined for this protein. This is the sequence of a model fit to electron density plots at 2.2 Angstroms resolution. The N-methylasparagine modification was omitted in the model.
Allophycocyanin is a photosynthetic bile pigment-protein complex with maximum absorption at approximately 650 nanometers.
Contains one covalently linked bilin chromophore.
PHYCOBILISOME 32.1 KDA LINKER POLYPEPTIDE, PHYCOCYANIN-ASSOCIATED, ROD 2
This protein is postulated to act both as terminal energy acceptor and as a linker polypeptide that stabilizes the phycobilisome architecture. May have intrinsic bilin lyase activity (By similarity).
Contains one covalently linked bilin chromophore. This protein autochromophorylates (Potential).
Belongs to the phycobilisome linker protein 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.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Key component of the proton channel; it may play 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, b and c.
ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL
This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.
Reversibly protonated during proton transport
ATP synthase alpha/beta chain, C-terminal domain
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
ATP synthase subunit alpha, chloroplastic
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 four main subunits: a, b, b' and c.
Belongs to the ATPase alpha/beta chains family.
ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
ATP synthase subunit beta, chloroplastic
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
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 four main subunits: a(1), b(1), b'(1) and c(9-12).
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). CF(0) has four main subunits: a(1), b(1), b'(1) 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, b and b' chains.
Belongs to the ATPase delta chain family.
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC
Epsilon subunit of F1F0-ATP synthase N-terminal domain
Produces ATP from ADP in the presence of a proton gradient across the membrane.
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). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
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 four main subunits: a(1), b(1), b'(1) 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, b and b' chains.
In plastids the F-type ATPase is also known as CF(1)CF(0).
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
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.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Biotin carboxyl carrier protein of acetyl-CoA carboxylase
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Binds 1 heme c group covalently per subunit.
The oxygen-evolving complex in red algae is composed of psbO (OEC33), psbQ', cytochrome c-550 and psbU.
Associated with photosystem II at the lumenal side of the thylakoid membrane.
Belongs to the cytochrome c family. PsbV subfamily.
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Unlike Synechococcus vulcanus it does not bind by itself to PSII, but requires all extrinsic members of the OEC.
Fumarate reductase/succinate dehydrogenase, transmembrane subunit
SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT
SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT, MITOCHONDRIAL
Fumarate reductase respiratory complex transmembrane subunits
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
The heme is bound between the two transmembrane subunits.
Forms part of complex II containing four subunits: a 70 kDa flavoprotein (FP), a 27 kDa iron-sulfur protein (IP), a cytochrome B and a membrane-anchoring protein.
ligand shared with second transmembrane subunit
Carbamoyl-phosphate synthase small subunit, N-terminal domain
CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN
Carbamoyl phosphate synthetase, small subunit N-terminal domain
Carbamoyl-phosphate synthase small chain
Carbamoyl-phosphate synthetase glutamine chain
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 LYS-79; TYR-113; GLU-137; ARG-193 AND ARG-238
AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN
Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic
Required for the expression of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo) (PubMed:18506097). ATPase involved in the activation of red-type RuBisCo, which tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP) (PubMed:27872295). Catalyzes the release of RuBP from inhibited RuBisCo in an ATP-dependent manner (PubMed:27872295). Activation of RuBisCO involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure (PubMed:27872295). The nuclear-encoded subunit plays a more critical role in activase function than the plastidial-encoded subunit (PubMed:27872295).
Forms homooligomers (PubMed:27872295). Forms heterohexameric rings with the plastid-encoded Rca subunit consisting of 3 of each nuclear- and plastidial-encoded subunits that alternate in the ring (PubMed:27872295).
Abolishes ATPase and activase activities.
Increases ATPase activity and abolishes activase activity.
CYTOCHROME C BIOGENESIS PROTEIN CCS1, CHLOROPLASTIC
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family.
CHLOROPLAST ENVELOPE MEMBRANE PROTEIN-RELATED
May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Necessary for the expression of RuBisCO.
Forms homooligomers (PubMed:27872295). Forms heterohexameric rings with the nuclear-encoded Rca subunit consisting of 3 of each nuclear- and plastidial-encoded subunits that alternate in the ring (PubMed:27872295).
Increases ATPase activity and reduces activase activity 5-fold.
Abolishes ATPase activity and slightly reduces activase activity.
Reduces ATPase activity 2-fold and activase activity 8-fold.
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.
Nitrogenase molybdenum iron protein domain
Proto-chlorophyllide reductase 57 kD subunit B
LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits.
ligand shared with heterodimeric partner
Magnesium chelatase subunit I, C-Terminal domain
MAGNESIUM-CHELATASE SUBUNIT CHLI-2, CHLOROPLASTIC
Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Belongs to the Mg-chelatase subunits D/I family.
LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.
LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N
ATP-dependent Clp protease ATP-binding subunit ClpA homolog
May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.
Cytochrome c oxidase-like, subunit I domain
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Binds 2 heme A groups non-covalently per subunit.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).
Belongs to the heme-copper respiratory oxidase family.
Cytochrome c oxidase subunit II-like, transmembrane region
Binds a dinuclear copper A center per subunit.
Belongs to the cytochrome c oxidase subunit 2 family.
Cytochrome c oxidase, subunit III, four-helix bundle
Belongs to the cytochrome c oxidase subunit 3 family.
Might function to covalently attach a chromophore to Cys residue(s) of phycobiliproteins.
Belongs to the CpcS/CpeS biliprotein lyase family.
Red alga, Porphyra yezoensis, cytochrome c550.
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Binds one heme group covalently by a single cysteine link with no axial amino acid ligand. This heme was named heme ci.
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer.
Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm.
Belongs to the cytochrome b family. PetB subfamily.
a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
The main subunits of complex b-c1 are: cytochrome b, cytochrome c1 and the Rieske protein.
Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.
The protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools.
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
Belongs to the cytochrome c family. PetJ subfamily.
Red alga, Porphyra yezoensis cytochrome c6.
Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer (By similarity).
Succinate dehydrogenase membrane anchor subunit
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins.
Complete sequence of the mitochondrial DNA of the red alga, Porphyra purpurea. Inverted repeats, sequence polymorphisms, and cyanobacterial introns.
This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Belongs to the helicase family. DnaB subfamily.
Probable replicative DNA helicase, 1st part
Probable replicative DNA helicase, 2nd part
Heat shock protein 70kD (HSP70), C-terminal subdomain
Heat shock protein 70kD (HSP70), peptide-binding domain
Belongs to the heat shock protein 70 family.
Cloning hsp70 from Porphyra haitanesis and Porphyra yezoensis.
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.
Expressed in both sporophyte and gametophyte phases of the life cycle.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Expressed only in the sporophyte, a shell-boring, filamentous phase.
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.
DNA helicase RuvA subunit, C-terminal domain
Cloning and analysis of the Porphyra yezoensis gene for tufA.
3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE
3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, CHLOROPLASTIC
Beta-ketoacyl-[acyl-carrier-protein] synthase III
3-oxoacyl-[acyl-carrier-protein] synthase 3
3-oxoacyl-[acyl-carrier-protein] synthase III
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Belongs to the thiolase-like superfamily. FabH family.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and thioredoxin.
Belongs to the 2Fe2S plant-type ferredoxin family.
Low-potential electron donor to a number of redox enzymes.
Ferredoxin thioredoxin reductase catalytic beta subunit
FERREDOXIN-THIOREDOXIN REDUCTASE CATALYTIC CHAIN, CHLOROPLASTIC
Ferredoxin thioredoxin reductase (FTR), catalytic beta chain
Ferredoxin-thioredoxin reductase, catalytic chain
Ferredoxin-thioredoxin reductase subunit B
Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin (By similarity).
Belongs to the ferredoxin thioredoxin reductase beta subunit family.
Increases the nucleophilicity of the active site Cys
ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1
Acts as a processive, ATP-dependent zinc metallopeptidase.
In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic
NADP-dependent glyceraldehydephosphate dehydrogenase
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]
GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED
Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
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.
NITROGEN REGULATORY PROTEIN P-II HOMOLOG
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme (By similarity).
Glutamate synthase, alpha subunit, C-terminal domain
FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE 1, CHLOROPLASTIC/MITOCHONDRIAL
Alpha subunit of glutamate synthase, C-terminal domain
Belongs to the glutamate synthase 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.
Mixed specificity lectin with anti-HIV activity. Binds to HIV envelope glycoproteins, including exterior membrane glycoprotein gp120, and inhibits viral entry into cells. Binding to gp120 is dependent on gp120 being glycosylated, and is inhibited by mannose, glucose and N-acetylglucosamine.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Acetylation is generally linked to gene activation. Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9ac is restricted to euchromatin (By similarity).
Methylated to form mainly H3K4me, H3K9me, H3K18me, H3K23me, H3K27me and H3K36me. H3K4me1/2/3, H3K9me3, H3K27me3 and H3K36me1/2/3 are typical marks for euchromatin, whereas heterochromatic chromocenters are enriched in H3K9me1/2 and H3K27me1/2. H2BK143ub1 is probably prerequisite for H3K4me (By similarity).
Can be phosphorylated to form H3S10ph, H3T11ph and H3S28ph.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me = methylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me = methylated Lys-10; H3S10ph = phosphorylated Ser-11; H3T11ph = phosphorylated Thr-12; H3K14ac = acetylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me = methylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me = methylated Lys-24; H3K27me = methylated Lys-28; H3S28ph = phosphorylated Ser-29; H3K36me = methylated Lys-37.
IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED
FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN
FAD-binding/transporter-associated domain-like
Catalyzes the selective oxidation of C1 hydroxyl moieties on mono- and disaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Hexose oxidase is able to oxidize a variety of substrates including D-glucose, D-galactose, maltose, cellobiose, and lactose.
Binds 1 FAD per subunit in a bicovalent manner.
0.3 mM for oxygen (at pH 5.8 and 25 degrees Celsius)
2.7 mM for D-glucose (at pH 6.3 and 25 degrees Celsius)
3.8 mM for D-galactose (at pH 6.3 and 25 degrees Celsius)
8.5 mM for glucose (at pH 5.8 and 25 degrees Celsius)
1.7 mM for lactose (at pH 5.8 and 25 degrees Celsius)
20 mM for galactose (at pH 5.8 and 25 degrees Celsius)
12.5 mM for cellobiose (at pH 5.8 and 25 degrees Celsius)
28 mM for maltose (at pH 5.8 and 25 degrees Celsius)
2.5 mM for glucose (at pH 6 and 26 degrees Celsius)
97 mM for lactose (at pH 6 and 26 degrees Celsius)
3.2 mM for galactose (at pH 6 and 26 degrees Celsius)
27 mM for cellobiose (at pH 6 and 26 degrees Celsius)
50 mM for maltose (at pH 6 and 26 degrees Celsius)
Optimum pH is 6 (PubMed:9108257, PubMed:11427234). A second pH optimum was found at pH 10 (PubMed:9108257, PubMed:11427234).
Cleaved into 40 kDa and 29 kDa cleavage products, but the 2 polypeptide chains do not separate and seem to be physically linked together.
The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Was initially reported to use Cu(2+) as a cofactor (PubMed:4708670). However, cofactor composition could not be confirmed later (PubMed:9108257), and the discrepancies in the reported characteristics of the enzyme were suggested to originate from the characterization of a contaminating protein in PubMed:4708670.
6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)
Loss of activity due to the absence of FAD cofactor.
Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae.
TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL
TRANSLATION INITIATION FACTOR IF-2-RELATED
Translation initiation factor IF-2, chloroplastic
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).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
Translation initiation factor IF- 2, domain 3
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
Translation initiation factor IF-3, chloroplastic
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.
Thiamin diphosphate-binding fold (THDP-binding)
Acetohydroxy-acid synthase large subunit
Binds 1 thiamine pyrophosphate per subunit.
ACETOLACTATE SYNTHASE SMALL SUBUNIT 2, CHLOROPLASTIC
Acetohydroxy-acid synthase small subunit
Belongs to the acetolactate synthase small subunit family.
Magnesium-dependent glutamate N-prenyltransferase
Kainic acid biosynthesis cluster protein A
Magnesium-dependent glutamate N-prenyltransferase: part of the gene cluster that mediates the biosynthesis of kainic acid (KA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins (PubMed:30995339). Catalyzes the conversion of L-glutamic acid (L-Glu) to prekainic acid in the presence of dimethylallyl diphosphate (DMAPP) (PubMed:30995339, PubMed:32457155). Can also use geranyl diphosphate (GPP) as substrate, thus leading to the formation of N-geranyl-L-glutamic acid (L-NGG) (PubMed:32457155, PubMed:30995339).
kcat is 0.29 min(-1) with geranyl diphosphate as substrate (PubMed:32457155). kcat is 1.3 min(-1) with dimethylallyl diphosphate as substrate (PubMed:32457155).
Increased affinity for geranyl diphosphate (GPP) leading to an enhanced catalytic efficiency with GPP as substrate, but reduced activity with dimethylallyl diphosphate (DMAPP).
2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED
Alpha-ketoglutarate dependent kainoid synthase
Kainic acid biosynthesis cluster protein C
Iron/ascorbate-dependent oxidoreductase: part of the gene cluster that mediates the biosynthesis of kainic acid (KA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins (PubMed:30995339). Catalyzes the conversion of prekainic acid to kainic acid and kainic acid lactone (PubMed:30995339).
Escherichia coli cells expressing Digenea simplex kabC are successfully converting supplied synthetic prekainic acid into kainic acid, thus providing a less expensive method to produce this molecule for neuro-pharmacological applications.
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Lectin specific for high mannose N-glycans, recognizes the branched moiety of these glycans. Does not recognize other types of N-glycans or monosaccharides. Agglutinates trypsin-treated sheep and rabbit erythrocytes and untreated sheep erythrocytes. Has mitogenic activity on mouse lymphocytes. Does not require metal ions for activity.
Stable over a wide pH range, activity is unaffected after incubation at pH 2.5-10.5.
Activity is unaffected by heating at 60 degrees Celsius for 1 hour. Activity gradually decreases after incubation at higher temperatures.
Lectin with specificity for complex N-linked glycans and O-linked glycans. Has hemagglutinating activity towards rabbit erythrocytes that is inhibited by N-acetyl-D-galactosamine.
Proteolytically cleaved. Major form may consist of cleaved, disulfide-bonded subunits.
The measured mass is that of the native single chain.
The measured mass is that of the reduced and carbamidomethylated single chain.
The measured mass is that of the reduced and carbamidomethylated N-terminal subunit.
The measured mass is that of the reduced and carbamidomethylated C-terminal subunit.
Interchain (between N-terminal and C-terminal subunits)
Lectin with specificity for complex N-linked glycans and O-linked glycans. Has hemagglutinating activity towards rabbit erythrocytes.
Proteolytically cleaved. Major mature form may consist of cleaved, disulfide-bonded N-terminal and C-terminal chains.
The measured mass is that of the reduced and carbamidomethylated N-terminal chain.
The measured mass is that of the reduced and carbamidomethylated C-terminal chain.
Lectin specific for high mannose N-glycans, recognizes the branched moiety of these glycans. Does not recognize other types of N-glycans or monosaccharides.
Lectin specific for core(alpha 1-6)fucosylated N-glycans. Inhibits platelet aggregation.
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.
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 in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. The target for the lipopolysaccharides produced in the chloroplast could either be the cell envelope of the eukaryote or the plastid membrane.
Belongs to the transferase hexapeptide repeat family. LpxA subfamily.
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. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. The target for the lipopolysaccharides produced in the chloroplast could either be the cell envelope of the eukaryote or the plastid membrane.
Lyase 2-enoyl-coa Hydratase, Chain A, domain 2
1,4-DIHYDROXY-2-NAPHTHOYL-COA SYNTHASE, PEROXISOMAL
Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.
Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily.
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.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3
Activating enzymes of the ubiquitin-like proteins
Probable molybdopterin-synthase adenylyltransferase
Molybdopterin-converting factor subunit 1 adenylase
Sulfur carrier protein MoaD adenylyltransferase
Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein moaD.
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Belongs to the complex I subunit 1 family.
Belongs to the complex I subunit 2 family.
NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
Belongs to the complex I subunit 3 family.
NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L
Belongs to the complex I subunit 4L family.
Belongs to the complex I subunit 4 family.
Belongs to the complex I subunit 5 family.
NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ
Belongs to the complex I subunit 6 family.
PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA
PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL
Pyruvate dehydrogenase E1 component subunit beta
YVTN repeat-like/Quinoprotein amine dehydrogenase
PHOTOSYSTEM II STABILITY/ASSEMBLY FACTOR HCF136, CHLOROPLASTIC
Oligoxyloglucan reducing end-specific cellobiohydrolase
Essential for photosystem II (PSII) biogenesis; required for assembly of an early intermediate in PSII assembly that includes D2 (psbD) and cytochrome b559.
Predicted to be imported into the lumen by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
A 7-bladed beta-propeller torus, about 54 by 55 Angstroms, with a depth of about 25 Angstroms and a central pore.
Belongs to the cytochrome b family. PetD subfamily.
PetG subunit of the cytochrome b6f complex
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex (By similarity).
PetL subunit of the cytochrome b6f complex
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
PetM subunit of the cytochrome b6f complex
PetN subunit of the cytochrome b6f complex
Polyenoic fatty acid isomerase from the marine alga Ptilota filicina.
Involved in the biosynthesis of conjugated triene-containing fatty acids. Catalyzes the isomerization of a wide range of substrates containing three or more methylene interrupted olefins into a Z,E,E conjugated triene functionality. May be involved in a stress tolerance mechanism as response to intertidal habitats with direct sunlight, desiccation and high temperature. In vitro substrates include arachidonic acid ((5Z,8Z,11Z,14Z)-eicosatetraenoic acid), EPA ((5Z,8Z, 11Z,14Z,17Z)-eicosapentaenoic acid), DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoic acid), adrenic acid ((7Z,10Z,13Z,16Z)-docosatetraenoic acid), anandamide (arachidonyl-N-ethanolamide) and eicosatrienoic acid ((5Z,8Z,11Z)-eicosatrienoic acid). Gamma-linolenic acid (18:3 6Z,9Z,12Z) and dihomo-gamma-linolenic acid (20:3 8Z,11Z,14Z) are transformed into mixtures of conjugated diene and triene fatty acids, linoleic acid is only transformed to a conjugated diene.
1.9 uM for (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoic acid
17.0 uM for (7Z,10Z,13Z,16Z)-docosatetraenoic acid
9.6 uM for (5Z,8Z, 11Z,14Z,17Z)-eicosapentaenoic acid
25.5 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid
52.8 uM for (5Z,8Z,11Z)-eicosatrienoic acid
1.84 umol/min/mg enzyme with (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoic acid as substrate
1.1 umol/min/mg enzyme with (7Z,10Z,13Z,16Z)-docosatetraenoic acid as substrate
6.0 umol/min/mg enzyme with (5Z,8Z, 11Z,14Z,17Z)-eicosapentaenoic acid as substrate
2.78 umol/min/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoic acid as substrate
0.31 umol/min/mg enzyme with (5Z,8Z,11Z)-eicosatrienoic acid as substrate
0.8 umol/min/mg enzyme with arachidonyl-N-ethanolamide as substrate
Optimum pH is below pH 6.0 with (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid as substrate.
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH APCB AND PHYCOCYANOBILIN
Neither a protein sequence nor a nucleotide sequence had been determined for this protein when the crystallographic structure was reported. The sequence of a model fit to electron density plots at 2.2 Angstroms resolution was used. When a nucleotide sequence became available, it replaced the model sequence. There are 14 differences between the model and the nucleotide sequences.
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
Heterodimer of an alpha and a beta subunit, which further assembles into trimers and the trimers into hexamers. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer.
The light-harvesting antenna system in red algae and cyanobacteria is formed of phycobilisomes. These are composed of the phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin (PCC). The phycobiliproteins all share the same subunit composition and organization with variations in the covalently bound open-chain tetrapyrrole chromophores. The phycobiliprotein complexes are arranged sequentially in antenna complexes linked by linker proteins with CPE at the periphery, CPC in the middle and APC at the core feeding to the photosynthetic reaction center.
Heme regulated photogenes in the unicellular rhodophyte, Cyanidium caldarium. Cloning and nucleotide sequence of genes for phycocyanin.
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CPCB AND PHYCOCYANOBILIN
Crystal Structure of C-Phycocyanin from Galdieria sulphuraria at 1.85 A.
High resolution structure of C-Phycocyanin from Galdieria sulphuraria reveals new insights of the Phycobilisome.
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
Heterodimer of an alpha and a beta subunit (Ref.1, PubMed:468790, PubMed:10354419). Dimers further assemble into trimers and the trimers into hexamers. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer (PubMed:10354419).
Cloning and sequence analysis of phycocyanin gene of Porphyra haitanensis.
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RPCB AND PHYCOCYANOBILIN
Heterodimer of an alpha and a beta subunit (PubMed:8168545). Dimers further assemble into trimers and the trimers into hexamers. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer (By similarity).
Cloning and sequence analysis of the genes encoding the a and b subunits of C-phycocyanin from the red alga Rhodella violacea.
Contains two covalently linked bilin chromophores.
Contains two covalently linked phycocyanobilin chromophores.
CHROMOPHORE ATTACHMENT AT CYS-82 AND CYS-153
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CPCA AND PHYCOCYANOBILIN
Heterodimer of an alpha and a beta subunit (PubMed:7028751, PubMed:468790, PubMed:10354419). Dimers further assemble into trimers and the trimers into hexamers. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer (PubMed:10354419).
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RPCA; PHYCOCYANOBILIN AND PHYCOERYTHROBILIN
Contains one covalently linked phycocyanobilin chromophore and one covalently linked phycoerythrobilin chromophore.
Heterodimer of an alpha and a beta chain (PubMed:8168545). Dimers further assemble into trimers and the trimers into hexamers. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer (By similarity).
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PHYCOERYTHROBILIN AND PHEB
Forms the periphery of the phycobilisome rod.
Contains two covalently linked phycoerythrobilin chromophores.
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PHYCOERYTHROBILIN AND CPEB
CHROMOPHORE BINDING AT ASN-47; LYS-81; CYS-82; ARG-84; HIS-88; ARG-137; CYS-139 AND ARG-142
Cloning and sequence analysis of phycoerythrin gene of Porphyra haitanensis.
Phycoerythrin encoding gene from Porphyra tenera.
Phycoerythrin encoding gene from Porphyra yezoensis.
Phycoerythrin-encoding gene from Porphyra yezoensis isolate Qingdao.
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PHEB AND PHYCOCYANOBILIN
Contains two covalently linked phycoerythrobilin chromophores. In PubMed:8876649 the authors refer to the bilins as phycoerythrobilins. In the PDB entries, the bilins are named as phycocyanobilins although the modeled compounds correspond to phycoerythrobilins.
CHROMOPHORE BINDING AT CYS-82 AND CYS-139
Heteromer of 6 alpha, 6 beta and one gamma chain.
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PHYCOERYTHROBILIN; PHYCOUROBILIN AND PHEA
Contains two covalently linked phycoerythrobilin chromophores and one covalently linked phycourobilin chromophore.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PHYCOERYTHROBILIN; PHYCOUROBILIN AND CPEA
Exhibits two smaller absorbance peaks at 544 nm and 495 nm.
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PHEA; PHYCOERYTHROBILIN AND PHYCOUROBILIN
CHROMOPHORE BINDING AT ASN-35; ASP-39; CYS-50; ASP-54; CYS-61; ASN-72; CYS-82 AND CYS-158
Contains two covalently linked phycoerythrobilin chromophores and one covalently linked phycourobilin chromophore. In the PDB entry, the bilins are named as phycocyanobilins although the modeled compounds correspond to phycoerythrobilins.
PROTEIN SEQUENCE OF 38-77; 79-84 AND 151-171
R-phycoerythrin gamma-1 chain, chloroplastic
Critical for the incorporation of phycoerythrin in the phycobilisome complex.
Heteromer of 6 alpha, 6 beta and 1 gamma chains.
Contains four covalently linked bilin chromophores.
R-phycoerythrin gamma chain, chloroplastic
Heteromer of 1 alpha, 1 beta and 2 gamma chains.
The full-length cDNA of R-phycoerythrin from Corallina officinalis.
Heteromer of 4 alpha, 4 beta and one gamma chains.
Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose (PubMed:9003801). GDP-mannose is an essential sugar nucleotide for the synthesis of D-mannose-containing cell wall polysaccharides (galactomannans and glucomannans), glycolipids, glycoproteins and the antioxidant L-ascorbate (Probable).
Glucose-1,6-bisphosphate or mannose-1,6-biphosphate are essential for activity.
ALL TRANS-POLYPRENYL-DIPHOSPHATE SYNTHASE PDSS1
Possible role in synthesis of the nonaprenyl side chain of plastoquinone or in synthesis of other prenyl chains such as undekaprenyl pyrophosphate.
Belongs to the FPP/GGPP synthase family.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM AND PHOSPHATE
Vanadium-containing Chloroperoxidase, domain 2
Acid phosphatase/Vanadium-dependent haloperoxidase
Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide.
Binds 1 Ca(2+) ion per subunit. The binding is important for enzyme stability.
Belongs to the vanadium-dependent haloperoxidase family.
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM AND PHOSPHATE
PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2
Photosystem I P700 chlorophyll a apoprotein A1
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits.
PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED
Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
The eukaryotic PSI reaction center is composed of at least 11 subunits.
Photosystem I PsaD, reaction center subunit II
PHOTOSYSTEM I REACTION CENTER SUBUNIT II
PHOTOSYSTEM I REACTION CENTER SUBUNIT II-1, CHLOROPLASTIC-RELATED
PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.
PHOTOSYSTEM I REACTION CENTER SUBUNIT IV A, CHLOROPLASTIC-RELATED
Photosystem I reaction center subunit IV
Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Photosystem I PsaF, reaction centre subunit III
PHOTOSYSTEM I REACTION CENTER SUBUNIT III, CHLOROPLASTIC
Subunit III of photosystem I reaction centre, PsaF
Photosystem I reaction center subunit III
Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI (By similarity).
Subunit VIII of photosystem I reaction centre, PsaI
Photosystem I reaction center subunit VIII
May help in the organization of the PsaL subunit.
PHOTOSYSTEM I REACTION CENTER SUBUNIT IX
Subunit IX of photosystem I reaction centre, PsaJ
May help in the organization of the PsaE and PsaF subunits.
Photosystem I reaction center subunit X, PsaK
Photosystem I reaction center subunit PsaK
Photosystem I PsaL, reaction centre subunit XI
PHOTOSYSTEM I REACTION CENTER SUBUNIT XI, CHLOROPLASTIC
Photosystem I reaction center subunit XI, PsaL
Photosystem I reaction center subunit XI
Subunit XII of photosystem I reaction centre, PsaM
Photosystem I reaction center subunit XII
PHOTOSYSTEM II REACTION CENTER PSB28 PROTEIN, CHLOROPLASTIC
Photosystem II reaction center Psb28 protein
Photosystem II reaction center W protein
Bacterial photosystem II reaction centre, L and M subunits
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
Belongs to the reaction center PufL/M/PsbA/D family.
Nucleotide sequence of psbA gene from Palmaria palmata.
Photosystem II CP47 reaction center protein
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Binds multiple chlorophylls. PSII binds additional chlorophylls, carotenoids and specific lipids.
Belongs to the PsbB/PsbC family. PsbB subfamily.
photosystem ii from thermosynechococcus elongatus
Photosystem II CP43 reaction center protein
Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Belongs to the PsbB/PsbC family. PsbC subfamily.
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Photosystem II cytochrome b559, alpha subunit
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Photosystem II reaction center protein H
Photosystem II 10 kDa phosphoprotein PsbH
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
PHOTOSYSTEM II REACTION CENTER PROTEIN I
Photosystem II reaction center protein I, PsbI
PHOTOSYSTEM II REACTION CENTER PROTEIN J
Photosystem II reaction center protein J, PsbJ
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PHOTOSYSTEM II REACTION CENTER PROTEIN K
Photosystem II reaction center protein K, PsbK
Photosystem II reaction center protein L, PsbL
Photosystem II reaction center protein L
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization.
May play a role in photosystem I and II biogenesis.
Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true.
PHOTOSYSTEM II REACTION CENTER PROTEIN T
Photosystem II reaction center protein T, PsbT
Seems to play a role in the dimerization of PSII.
Photosystem II 12 kDa extrinsic protein, chloroplastic
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation (By similarity). Does not bind by itself to PSII; it requires all other members of the OEC.
Predicted to be translocated into the thylakoid lumen by the Tat system. The position of the first transit peptide cleavage has not been experimentally proven.
Gj536 Griffithsia japonica photosystem II 12 kDa extrinsic protein gene.
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Predicted to be translocated into the thylakoid lumen by the Tat system. The position of the transit peptide cleavages have not been experimentally proven.
The research on genes expression pattern of Porphyra yezoensis based on cDNA microarray.
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-152
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation (By similarity).
Predicted to be translocated into the thylakoid lumen by the Tat system.
Photosystem II reaction center X protein
Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
PSII consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes.
Belongs to the PsbX family. Type 1 subfamily.
Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
PHOTOSYSTEM II REACTION CENTER PROTEIN Z
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Associated with the photosystem II complex.
Phycobilisome rod-core linker polypeptide cpcG
Rod-core linker protein required for attachment of phycocyanin to allophycocyanin in cores of phycobilisomes.
Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
The phycobilisome is a hemidiscoidal structure that is composed of two distinct substructures: a core complex and a number of rods radiating from the core.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Probable RuBisCO transcriptional regulator
Trans-acting transcriptional regulator of RuBisCO genes (rbcL and rbcS) expression.
Belongs to the LysR transcriptional regulatory family.
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
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 in the photorespiration process. 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.
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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity).
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' (By similarity).
A thioredoxin gene is located upstream of rbcLS in the unicellular red alga Cyanidium caldarium, strain RK-1.
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF UNACTIVATED HOLOENZYME IN COMPLEX WITH O2 OR CO2 AND MAGNESIUM
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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (Probable). Carbon dioxide and oxygen bind in the same pocket of the enzyme in a similar manner (PubMed:23112176).
Species determination utilizing Porphyra (Rhodophyta) plastid DNA RuBisCo sequences.
A comparison of the phylogenetic relationships of Porphyra from the coast of New England inferred from rbcL and 18S ribosomal RNA.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-488
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-488
Ribulose bisphosphate carboxylase, small subunit
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT
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 in the photorespiration process. 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.
In this alga, in contrast to plants, the small subunit is encoded in the chloroplast.
Belongs to the RuBisCO small chain family.
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 in the photorespiration process. 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. Carbon dioxide and oxygen bind in the same pocket of the enzyme in a similar manner (PubMed:23112176).
Ribosomal protein L11, C-terminal domain
Ribosomal protein L11/L12, N-terminal domain
39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL
50S ribosomal protein L11, chloroplastic
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.
Belongs to the universal ribosomal protein uL11 family.
39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL
Ribosomal protein L7/12, oligomerisation (N-terminal) domain
50S ribosomal protein L12, chloroplastic
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.
39S RIBOSOMAL PROTEIN L13, MITOCHONDRIAL
50S ribosomal protein L13, chloroplastic
Belongs to the universal ribosomal protein uL13 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl13.
54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL
50S ribosomal protein L14, chloroplastic
Belongs to the universal ribosomal protein uL14 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl14.
39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL
50S ribosomal protein L16, chloroplastic
Belongs to the universal ribosomal protein uL16 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl16.
39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL
50S ribosomal protein L18, chloroplastic
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
Part of the 50S ribosomal subunit; contacts the 5S rRNA.
Belongs to the universal ribosomal protein uL18 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl18.
39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL
50S ribosomal protein L19, chloroplastic
Belongs to the bacterial ribosomal protein bL19 family.
Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential).
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 (By similarity).
Belongs to the bacterial ribosomal protein bL20 family.
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.
50S RIBOSOMAL PROTEIN L21, CHLOROPLASTIC
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.
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.
Cloning and analysis of the Porphyra yezoensis gene for rpl22.
50S ribosomal protein L23, chloroplastic
Belongs to the universal ribosomal protein uL23 family.
RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN
50S RIBOSOMAL PROTEIN L24, CHLOROPLASTIC
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.
Belongs to the universal ribosomal protein uL24 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl24.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
50S ribosomal protein L27, chloroplastic
Belongs to the bacterial ribosomal protein bL27 family.
50S ribosomal protein L28, chloroplastic
Belongs to the bacterial ribosomal protein bL28 family.
39S RIBOSOMAL PROTEIN L28, MITOCHONDRIAL
50S RIBOSOMAL PROTEIN L29, CHLOROPLASTIC
60S RIBOSOMAL PROTEIN L35/50S RIBOSOMAL PROTEIN L29
Belongs to the universal ribosomal protein uL29 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl29.
Belongs to the universal ribosomal protein uL2 family.
50S RIBOSOMAL PROTEIN L31, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Cloning and analysis of the Porphyra yezoensis gene for rpl31.
50S ribosomal protein L32, chloroplastic
Belongs to the bacterial ribosomal protein bL32 family.
50S RIBOSOMAL PROTEIN L33, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL33 family.
50S ribosomal protein L34, chloroplastic
Belongs to the bacterial ribosomal protein bL34 family.
50S ribosomal protein L35, chloroplastic
Belongs to the bacterial ribosomal protein bL35 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32
50S RIBOSOMAL PROTEIN L36, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL36 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl36.
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.
Belongs to the universal ribosomal protein uL3 family.
Belongs to the universal ribosomal protein uL4 family.
Belongs to the universal ribosomal protein uL5 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl5.
Belongs to the universal ribosomal protein uL6 family.
Cloning and analysis of the Porphyra yezoensis gene for rpl6.
Belongs to the bacterial ribosomal protein bL9 family.
Gj179 Griffithsia japonica ribosome protein L14 gene.
Belongs to the eukaryotic ribosomal protein eL14 family.
60S ribosomal protein L16, mitochondrial
Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
5' to 3' exonuclease, C-terminal subdomain
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
Plastid-encoded RNA polymerase subunit alpha
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) 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.
Cloning and analysis of the Porphyra yezoensis gene for rpoA.
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
Plastid-encoded RNA polymerase subunit beta
Belongs to the RNA polymerase beta chain family.
DNA-directed RNA polymerase subunit beta'
Plastid-encoded RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-245
DNA-directed RNA polymerase subunit beta''
Plastid-encoded RNA polymerase subunit beta''
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity).
DNA-directed RNA polymerase subunit beta'-beta''
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. Beta' and beta'' are fused in this algae.
In this algae the rpoC1 (beta') and rpoC2 (beta'') genes are fused into one ORF. This seems to be the result of evolution acting to reduce protein size rather than horizontal transfer from a bacteria. Thus this is considered an atypical member of the bacterial RpoC family.
In the N-terminal section; belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
In the C-terminal section; belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
Putative DNA-directed RNA polymerase subunit omega
Plastid-encoded RNA polymerase omega subunit
May be involved in RNA polymerase activity.
Belongs to the RNA polymerase subunit omega family.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
30S ribosomal protein S10, chloroplastic
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
Cloning and analyzing of Porphyra yezoensis gene for 30S ribosomal protein S10.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
30S ribosomal protein S11, chloroplastic
Belongs to the universal ribosomal protein uS11 family.
Cloning and analysis of the Porphyra yezoensis gene for rps11.
28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL
28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL
30S ribosomal protein S12, chloroplastic
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity).
Belongs to the universal ribosomal protein uS12 family.
Cloning and analysis of the Porphyra yezoensis gene for rps12.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL
30S ribosomal protein S13, chloroplastic
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.
Belongs to the universal ribosomal protein uS13 family.
Cloning and analysis of the Porphyra yezoensis gene for rps13.
30S ribosomal protein S13-2, chloroplastic
28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL
Glucocorticoid receptor-like (DNA-binding domain)
30S ribosomal protein S14, chloroplastic
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the universal ribosomal protein uS14 family.
28S RIBOSOMAL PROTEIN S16, MITOCHONDRIAL
30S ribosomal protein S16, chloroplastic
Belongs to the bacterial ribosomal protein bS16 family.
37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL
30S ribosomal protein S17, chloroplastic
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.
Cloning and analysis of the Porphyra yezoensis gene for rps17.
28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL
30S ribosomal protein S18, chloroplastic
Belongs to the bacterial ribosomal protein bS18 family.
37S RIBOSOMAL PROTEIN S19, MITOCHONDRIAL
30S ribosomal protein S19, chloroplastic
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
Cloning and analysis of the Porphyra yezoensis gene for rps19.
Belongs to the bacterial ribosomal protein bS1 family.
30S RIBOSOMAL PROTEIN S20, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bS20 family.
30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR
Belongs to the universal ribosomal protein uS2 family.
Prokaryotic type KH domain (KH-domain type II)
Belongs to the universal ribosomal protein uS3 family.
Cloning and analysis of the Porphyra yezoensis gene for rps3.
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.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity).
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 88-168
With S4 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S4 (By similarity).
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.
Cloning and analysis of the Porphyra yezoensis gene for rps5.
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.
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.
Belongs to the universal ribosomal protein uS8 family.
Cloning and analysis of the Porphyra yezoensis gene for rps8.
Belongs to the universal ribosomal protein uS9 family.
Cloning and analysis of the Porphyra yezoensis gene for rps9.
30S RIBOSOMAL PROTEIN 3-1, CHLOROPLASTIC
Probably a ribosomal protein or a ribosome-associated protein.
Belongs to the chloroplast-specific ribosomal protein cS23 family.
Gj569 Griffithsia japonica ribosome protein S29 gene.
Belongs to the eukaryotic ribosomal protein eS8 family.
Protein S12 is involved in the translation initiation step.
Cloning of cDNA coding for ATP-sulfurylase of Porphyra yezoensis.
Inhibited by adenosine 5'-phosphosulfate (APS), but not by 3'phosphoadenosine 5'-phosphosulfate (PAPS). Inhibited by AMP, ADP, CTP, GTP, ITP, UTP and anions other than those in group IV.
Optimum temperature is 37 degrees Celsius.
Belongs to the sulfate adenylyltransferase family.
SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL
SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Helical scaffold and wing domains of SecA
SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM
Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
A minor fraction is associated with the chloroplast thylakoid membrane.
Probable protein-export membrane protein secG
Involved in protein export. Participates in an early event of protein translocation across the chloroplast thylakoid membrane (Potential).
PREPROTEIN TRANSLOCASE SUBUNIT SCY2, CHLOROPLASTIC
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Component of the plastid Sec protein translocase complex, which is composed of at least SecY and SecE.
the general secretory pathway (sec) family
Bioinformatics prediction programs detect only 9 instead of 10 transmembrane regions.
The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Bioinformatics prediction programs detect only 8 instead of 10 transmembrane regions.
Cloning and analysis of the Porphyra yezoensis gene for secY.
Component of the plastid Sec protein translocase complex, which is composed of at least SecY, SecE and SecG.
S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC
Uroporphyrinogen-III C-methyltransferase
S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase
Catalyzes the two successive C-2 and C-7 methylation reactions involved in the conversion of uroporphyrinogen III to precorrin-2 via the intermediate formation of precorrin-1. It is a step in the biosynthesis of both cobalamin (vitamin B12) and siroheme.
Belongs to the precorrin methyltransferase family.
Ferrodoxin-fold anticodon-binding domain
Phenylalanyl-trna Synthetase, Chain B, domain 3
PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47
Phenylalanine--tRNA ligase beta subunit, chloroplastic
Phenylalanyl-tRNA synthetase beta subunit
Tetramer of two alpha and two beta subunits.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
Belongs to the class-II aminoacyl-tRNA synthetase family.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Expression of beta-tubulin genes in the sporophyte and gametophyte of the red alga Porphyra purpurea.
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.
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Adenine nucleotide alpha hydrolases-like
tRNA(Ile)-lysidine synthase, chloroplastic
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Belongs to the tRNA(Ile)-lysidine synthase family.
In plants, there are two types of TPIS, cytosolic and plastid.
Belongs to the triosephosphate isomerase 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.
MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN
MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED
Anthranilate synthase, glutamine amidotransferase component
Tetramer of two components I and two components II.
Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
Uracil phosphoribosyltransferase homolog
V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).
ATP-SYNT_AB DOMAIN-CONTAINING PROTEIN-RELATED
Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Photosystem II reaction center protein Ycf12
A core subunit of photosystem II (PSII).
Possible role in chlorophyll and/or carotenoid binding.
PROTEIN COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB3, CHLOROPLASTIC-RELATED
PROTEIN TRIGALACTOSYLDIACYLGLYCEROL 2, CHLOROPLASTIC
UPF0051 PROTEIN ABCI8, CHLOROPLASTIC-RELATED
Histidine kinase-like ATPase, C-terminal domain
ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Homodimeric domain of signal transducing histidine kinase
Uncharacterized sensor-like histidine kinase ycf26
C-terminal effector domain of the bipartite response regulators
Probable transcriptional regulator ycf27
Probable promoter-specific protein mediating the interaction between DNA and RNA polymerase.
Putative HTH-type transcriptional regulator ycf28
HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C
Probable transcriptional regulator ycf29
RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN
PROTEIN CONSERVED IN THE GREEN LINEAGE AND DIATOMS 27, CHLOROPLASTIC
Belongs to the ABC-2 integral membrane protein family.
PROTEIN HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244, CHLOROPLASTIC
Belongs to the NmrA-type oxidoreductase family. Ycf39 subfamily.
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Putative single-stranded DNA-binding protein ycf41
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Homodimer; disulfide-linked, upon oxidation.
The Cys-53-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-53 (probably Cys-SOH) rapidly reacts with Cys-174-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin (By similarity).
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Cysteine sulfenic acid (-SOH) intermediate
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED
P-LOOP CONTAINING NUCLEOSIDE TRIPHOSPHATE HYDROLASES SUPERFAMILY PROTEIN
Uncharacterized AAA domain-containing protein ycf46
Belongs to the AAA ATPase family. Highly divergent.
Seems to be required for the assembly of the photosystem I complex.
Uncharacterized N-acetyltransferase ycf52
Belongs to the acetyltransferase family. Ycf52 subfamily.
TETRAPYRROLE-BINDING PROTEIN, CHLOROPLASTIC
Ribonuclease Z/Hydroxyacylglutathione hydrolase-like
MlaE family lipid ABC transporter permease subunit
ABC TRANSPORTER PERMEASE PROTEIN-RELATED
PROTEIN TRIGALACTOSYLDIACYLGLYCEROL 1, CHLOROPLASTIC
Probable ABC transporter permease protein ycf63
Could be part of an ABC transporter complex.
GLUTAREDOXIN-RELATED PROTEIN 5, MITOCHONDRIAL
Uncharacterized monothiol glutaredoxin ycf64
Belongs to the glutaredoxin family. Monothiol subfamily.
iron-sulfur cluster assembly accessory protein
IRON-SULFUR ASSEMBLY PROTEIN ISCA, CHLOROPLASTIC
Belongs to the HesB/IscA family. Ycf83 subfamily.
Uncharacterized protein in rpl9-rpl11 intergenic region
CYTOCHROME C-TYPE BIOGENESIS CCDA-LIKE CHLOROPLASTIC PROTEIN
CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED
Putative cytochrome c-type biogenesis protein DbsD-like
Could be involved in cytochrome c synthesis.