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 24-JAN-2024, entry version 157. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P23577; -. DR PaxDb; 3055-DAA00904; -. DR GeneID; 2716989; -. DR KEGG; cre:ChreCp001; -. DR eggNOG; ENOG502QPT8; Eukaryota. DR HOGENOM; CLU_033498_0_0_1; -. DR InParanoid; P23577; -. DR BioCyc; CHLAMY:CHRECP001-MONOMER; -. DR BioCyc; MetaCyc:CHRECP001-MONOMER; -. 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: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; 2.40.50.100; -; 1. DR Gene3D; 2.60.40.830; Cytochrome f large domain; 1. DR Gene3D; 1.20.5.700; Single helix bin; 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 PANTHER; PTHR33288; -; 1. DR PANTHER; PTHR33288:SF10; CYTOCHROME F; 1. DR Pfam; PF01333; Apocytochr_F_C; 1. DR Pfam; PF16639; Apocytochr_F_N; 1. DR PRINTS; PR00610; CYTOCHROMEF. DR SUPFAM; SSF103431; Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor; 1. DR SUPFAM; SSF49441; Cytochrome f, large domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 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 //