CYF_CHLRE
ID CYF_CHLRE Reviewed; 317 AA.
AC P23577; B7U1E4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=2060646; DOI=10.1016/0014-5793(91)80698-3;
RA Bueschlen S., Choquet Y., Kuras R., Wollman F.A.;
RT "Nucleotide sequences of the continuous and separated petA, petB and petD
RT chloroplast genes in Chlamydomonas reinhardtii.";
RL FEBS Lett. 284:257-262(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cw15;
RA Matsumoto T., Matsuo M., Matsuda Y.;
RT "Structural analysis and expression during dark-light transitions of a gene
RT for cytochrome f in Chlamydomonas reinhardtii.";
RL Plant Cell Physiol. 32:863-872(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1868213; DOI=10.1007/bf00036814;
RA Bertsch J., Malkin R.;
RT "Nucleotide sequence of the petA (cytochrome f) gene from the green alga,
RT Chlamydomonas reinhardtii.";
RL Plant Mol. Biol. 17:131-133(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [5]
RP PROTEIN SEQUENCE OF 32-53, AND CHARACTERIZATION.
RC STRAIN=WT12;
RX PubMed=7493968; DOI=10.1074/jbc.270.49.29342;
RA Pierre Y., Breyton C., Kramer D., Popot J.-L.;
RT "Purification and characterization of the cytochrome b6 f complex from
RT Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 270:29342-29349(1995).
RN [6]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 32-282 IN COMPLEX WITH HEME, AND
RP COFACTOR.
RX PubMed=10869174; DOI=10.1021/bi000090k;
RA Chi Y.-I., Huang L.-S., Zhang Z., Fernandez-Velasco J.G., Berry E.A.;
RT "X-ray structure of a truncated form of cytochrome f from Chlamydomonas
RT reinhardtii.";
RL Biochemistry 39:7689-7701(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 32-282 IN COMPLEX WITH HEME, AND
RP COFACTOR.
RX PubMed=10924110; DOI=10.1021/bi0004596;
RA Sainz G., Carrell C.J., Ponamarev M.V., Soriano G.M., Cramer W.A.,
RA Smith J.L.;
RT "Interruption of the internal water chain of cytochrome f impairs
RT photosynthetic function.";
RL Biochemistry 39:9164-9173(2000).
CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC electron transfer between photosystem II (PSII) and photosystem I
CC (PSI), cyclic electron flow around PSI, and state transitions.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:10869174, ECO:0000269|PubMed:10924110};
CC Note=Binds 1 heme group covalently. {ECO:0000269|PubMed:10869174,
CC ECO:0000269|PubMed:10924110};
CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC PetN. The complex functions as a dimer.
CC -!- INTERACTION:
CC P23577; Q84V18: STT7; NbExp=5; IntAct=EBI-9013553, EBI-15762546;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR EMBL; X72917; CAA51422.1; -; Genomic_DNA.
DR EMBL; D01036; BAA00844.1; -; Genomic_DNA.
DR EMBL; X57744; CAA40911.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50091.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00904.1; -; Genomic_DNA.
DR PIR; S16916; S16916.
DR RefSeq; NP_958358.1; NC_005353.1.
DR PDB; 1CFM; X-ray; 2.00 A; A/B/C=32-282.
DR PDB; 1E2V; X-ray; 1.85 A; A/B/C=32-282.
DR PDB; 1E2W; X-ray; 1.60 A; A/B=32-282.
DR PDB; 1E2Z; X-ray; 2.50 A; A/B/C=32-282.
DR PDB; 1EWH; X-ray; 2.35 A; A/B/C=32-282.
DR PDB; 1Q90; X-ray; 3.10 A; A=32-317.
DR PDBsum; 1CFM; -.
DR PDBsum; 1E2V; -.
DR PDBsum; 1E2W; -.
DR PDBsum; 1E2Z; -.
DR PDBsum; 1EWH; -.
DR PDBsum; 1Q90; -.
DR AlphaFoldDB; P23577; -.
DR SMR; P23577; -.
DR DIP; DIP-48404N; -.
DR IntAct; P23577; 5.
DR STRING; 3055.DAA00904; -.
DR PaxDb; P23577; -.
DR PRIDE; P23577; -.
DR GeneID; 2716989; -.
DR KEGG; cre:ChreCp001; -.
DR eggNOG; ENOG502QPT8; Eukaryota.
DR HOGENOM; CLU_033498_0_0_1; -.
DR InParanoid; P23577; -.
DR OrthoDB; 826802at2759; -.
DR BioCyc; MetaCyc:CHRECP001-MON; -.
DR BRENDA; 7.1.1.6; 1318.
DR EvolutionaryTrace; P23577; -.
DR Proteomes; UP000006906; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.830; -; 1.
DR HAMAP; MF_00610; Cytb6_f_cytF; 1.
DR InterPro; IPR024058; Cyt-f_TM.
DR InterPro; IPR002325; Cyt_f.
DR InterPro; IPR024094; Cyt_f_lg_dom.
DR InterPro; IPR036826; Cyt_f_lg_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF01333; Apocytochr_F_C; 1.
DR Pfam; PF16639; Apocytochr_F_N; 1.
DR PRINTS; PR00610; CYTOCHROMEF.
DR SUPFAM; SSF103431; SSF103431; 1.
DR SUPFAM; SSF49441; SSF49441; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR PROSITE; PS51010; CYTF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Photosynthesis; Plastid;
KW Reference proteome; Signal; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:7493968"
FT CHAIN 32..317
FT /note="Cytochrome f"
FT /id="PRO_0000023809"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:10869174,
FT ECO:0000269|PubMed:10924110"
FT BINDING 52
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:10869174,
FT ECO:0000269|PubMed:10924110"
FT BINDING 55
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:10869174,
FT ECO:0000269|PubMed:10924110"
FT BINDING 56
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:10869174,
FT ECO:0000269|PubMed:10924110"
FT CONFLICT 53
FT /note="A -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="I -> S (in Ref. 3; CAA40911)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..91
FT /note="KQV -> NS (in Ref. 3; CAA40911)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="Y -> F (in Ref. 3; CAA40911)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="D -> Y (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1E2W"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1E2Z"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1E2W"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1E2W"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1E2W"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1E2W"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 174..186
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1Q90"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1E2W"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1E2V"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:1E2W"
FT HELIX 280..314
FT /evidence="ECO:0007829|PDB:1Q90"
SQ SEQUENCE 317 AA; 34292 MW; 1DC74E50552B7A53 CRC64;
MSNQVFTTLR AATLAVILGM AGGLAVSPAQ AYPVFAQQNY ANPREANGRI VCANCHLAQK
AVEIEVPQAV LPDTVFEAVI ELPYDKQVKQ VLANGKKGDL NVGMVLILPE GFELAPPDRV
PAEIKEKVGN LYYQPYSPEQ KNILVVGPVP GKKYSEMVVP ILSPDPAKNK NVSYLKYPIY
FGGNRGRGQV YPDGKKSNNT IYNASAAGKI VAITALSEKK GGFEVSIEKA NGEVVVDKIP
AGPDLIVKEG QTVQADQPLT NNPNVGGFGQ AETEIVLQNP ARIQGLLVFF SFVLLTQVLL
VLKKKQFEKV QLAEMNF
