NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
The complete sequence of the cyanelle genome of Cyanophora paradoxa: the genetic complexity of a primitive plastid.
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.
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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15
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.
Allophycocyanin is a photosynthetic bile pigment-protein complex with maximum absorption at approximately 650 nanometers.
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.
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
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
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.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Belongs to the ATPase epsilon chain family.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). 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.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Reversibly protonated during proton transport
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.
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.
TCP-1-like chaperonin intermediate domain
60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Belongs to the chaperonin (HSP60) family.
Nitrogenase molybdenum iron protein domain
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 PROTEOLYTIC SUBUNIT
ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT, MITOCHONDRIAL
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
Component of the chloroplastic Clp protease core complex.
Putative ATP-dependent Clp protease proteolytic subunit-like
Has lost the two conserved residues (Ser and His) proposed to be part of the active site. Therefore it could be inactive.
Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Belongs to the FPP/GGPP synthase family.
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Binds 1 heme c group covalently per subunit.
With psbO and psbU forms the oxygen-evolving complex of photosystem II.
Associated with photosystem II at the lumenal side of the thylakoid membrane.
Belongs to the cytochrome c family. PsbV subfamily.
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 (By similarity).
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.
Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor
Heat shock protein 70kD (HSP70), peptide-binding domain
Belongs to the heat shock protein 70 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-409
EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
Ferredoxin reductase-like, C-terminal NADP-linked domain
May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
Belongs to the ferredoxin--NADP reductase type 1 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.
PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FTSW-RELATED
Putative peptidoglycan glycosyltransferase FtsW
Could play a role in cyanelle division/peptidoglycan biosynthesis.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 407-432
Glutamyl-tRNA reductase, N-terminal domain
GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC
Glutamyl tRNA-reductase catalytic, N-terminal domain
Glutamyl tRNA-reductase dimerization domain
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Belongs to the glutamyl-tRNA reductase family.
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).
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Belongs to the quinolinate synthase family. Type 2 subfamily.
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.
Associated with a PSII precusor complex on the lumenal side of the thylakoid membrane.
A 7-bladed beta-propeller torus, about 55 by 55 Angstroms, with a depth of about 25 Angstroms and a central pore.
a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
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.
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.
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
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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-172
Contains two covalently linked phycocyanobilin chromophores.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46
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.
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 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 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.
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 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 cytochrome c6 (By similarity).
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 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.
Nucleotide sequence of a cDNA encoding the entire precursor polypeptide for the 20 kDa PS I polypeptide of the photosystem I reaction center from Cyanophora paradoxa.
Photosystem I PsaD, reaction center subunit II
PHOTOSYSTEM I REACTION CENTER SUBUNIT II
PHOTOSYSTEM I REACTION CENTER SUBUNIT II-1, CHLOROPLASTIC-RELATED
Photosystem I reaction center subunit II, cyanelle
PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein (By similarity).
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.
The soluble domain is associated with the lumenal side of the thylakoid membrane.
PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII
Subunit VIII of photosystem I reaction centre, PsaI
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.
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.
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.
PHOTOSYSTEM II REACTION CENTER PROTEIN M
Photosystem II reaction center protein M, PsbM
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.
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, cyanelle
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
With PsbO and PsbV forms the oxygen-evolving complex of photosystem II. This protein is not detected by antibodies against green algal PsbU but it is detected by antibodies against red algal PsbU (PubMed:16176274).
Might be translocated into the thylakoid lumen by the Tat system. The position of the transit peptide cleavages have not been experimentally proven.
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.
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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 471-475
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.
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. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Heterohexadecamer of 8 large and 8 small subunits.
Belongs to the RuBisCO small chain family.
Ribosomal protein L11, C-terminal domain
Ribosomal protein L11/L12, N-terminal domain
39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the universal ribosomal protein uL11 family.
39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL
Ribosomal protein L7/12, oligomerisation (N-terminal) domain
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
Belongs to the bacterial ribosomal protein bL12 family.
54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL
Belongs to the universal ribosomal protein uL14 family.
39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL
Belongs to the universal ribosomal protein uL16 family.
39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL
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.
39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Belongs to the bacterial ribosomal protein bL19 family.
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.
50S RIBOSOMAL PROTEIN L21, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL21 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-114
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.
39S RIBOSOMAL PROTEIN L28, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bL28 family.
Belongs to the universal ribosomal protein uL2 family.
50S RIBOSOMAL PROTEIN L33, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL33 family.
Belongs to the bacterial ribosomal protein bL34 family.
Belongs to the bacterial ribosomal protein bL35 family.
50S RIBOSOMAL PROTEIN L36, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL36 family.
50S RIBOSOMAL PROTEIN L3-1, CHLOROPLASTIC
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the universal ribosomal protein uL3 family.
Belongs to the universal ribosomal protein uL5 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41
Belongs to the universal ribosomal protein uL6 family.
Belongs to the universal ribosomal protein uL13 family.
Belongs to the eukaryotic ribosomal protein eL21 family.
Belongs to the eukaryotic ribosomal protein eL31 family.
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.
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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-244
DNA-directed RNA polymerase subunit beta'
Plastid-encoded RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
DNA-directed RNA polymerase subunit beta''
Plastid-encoded RNA polymerase subunit beta''
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
Belongs to the universal ribosomal protein uS11 family.
28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL
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.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.
Belongs to the universal ribosomal protein uS13 family.
28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL
Glucocorticoid receptor-like (DNA-binding domain)
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the universal ribosomal protein uS14 family.
28S RIBOSOMAL PROTEIN S16, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bS16 family.
37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS17 family.
28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bS18 family.
37S RIBOSOMAL PROTEIN S19, MITOCHONDRIAL
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
30S RIBOSOMAL PROTEIN S20, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bS20 family.
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.
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 (By similarity).
Belongs to the universal ribosomal protein uS4 family.
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.
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.
Belongs to the universal ribosomal protein uS9 family.
Cloning of a cDNA encoding the S12 ribosomal protein from Cyanophora paradoxa.
Belongs to the eukaryotic ribosomal protein eS12 family.
Cyanophora paradoxa mRNA for 40S subunit ribosomal protein.
Belongs to the eukaryotic ribosomal protein eS21 family.
the general secretory pathway (sec) family
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 (By similarity).
Component of the Sec protein translocase complex, which is composed of at least SecY and SecE.
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.
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.
CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL
CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED
Cytochrome b6-f complex iron-sulfur subunit 1, cyanelle
Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein 1
The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer.
This protein is 1 of 2 subunits of the cytochrome b6-f complex that are encoded in the nucleus.
The Rieske iron-sulfur protein is a high potential 2Fe-2S protein.
Belongs to the Rieske iron-sulfur protein family.
Cytochrome b6-f complex iron-sulfur subunit 2, cyanelle
Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein 2
Photosystem II reaction center protein Ycf12
A core subunit of photosystem II (PSII).
Possible role in chlorophyll and/or carotenoid binding.
UPF0051 PROTEIN ABCI8, CHLOROPLASTIC-RELATED
Probable transcriptional regulator ycf27
Probable promoter-specific protein mediating the interaction between DNA and RNA polymerase.
C-terminal effector domain of the bipartite response regulators
Probable transcriptional regulator ycf29
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.
Seems to be required for the assembly of the photosystem I complex.
Recombination protein O, C-terminal domain
Uncharacterized 24.3 kDa protein in hemA-psbN intergenic region
Uncharacterized 24.3 kDa protein in psbH-rpl11 intergenic region
Uncharacterized 3.4 kDa protein in atpE-petA intergenic region
Uncharacterized protein in petA-psaM intergenic region
Uncharacterized 5.7 kDa protein in psbM-psbX intergenic region
Uncharacterized 21.2 kDa protein in psbX-ycf33 intergenic region
Uncharacterized 9.4 kDa protein in trpG-ccsA intergenic region
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-299
ABC transporter involved in vitamin B12 uptake, BtuC
IRON TRANSPORT SYSTEM MEMBRANE PROTEIN HI_0359-RELATED
Uncharacterized membrane protein in ycf23-apcF intergenic region
Belongs to the ABC-3 integral membrane protein family.
IRON TRANSPORT SYSTEM ATP-BINDING PROTEIN HI_0361-RELATED
METAL TRANSPORT SYSTEM ATP-BINDING PROTEIN TM_0124-RELATED
Probable ABC transporter ATP-binding protein in ycf23-apcF intergenic region
Belongs to the ABC transporter superfamily.
Uncharacterized 21.2 kDa protein in ycf23-apcF intergenic region
Uncharacterized 11.2 kDa protein in ycf23-apcF intergenic region