ID   CYF_SPIOL               Reviewed;         320 AA.
AC   P16013; Q9M3L3;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA;
OS   Spinacia oleracea (Spinach).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Alt J., Herrmann R.G.;
RT   "Nucleotide sequence of the gene for pre-apocytochrome f in the spinach
RT   plastid chromosome.";
RL   Curr. Genet. 8:551-557(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX   PubMed=11292076; DOI=10.1023/a:1006478403810;
RA   Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA   Mache R.;
RT   "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT   sequence and gene organization.";
RL   Plant Mol. Biol. 45:307-315(2001).
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       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group covalently. {ECO:0000250};
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR   EMBL; M36602; AAA84632.1; -; Genomic_DNA.
DR   EMBL; AJ400848; CAB88742.1; -; Genomic_DNA.
DR   PIR; S00430; S00430.
DR   RefSeq; NP_054949.1; NC_002202.1.
DR   PDB; 6RQF; EM; 3.58 A; C/K=36-320.
DR   PDBsum; 6RQF; -.
DR   AlphaFoldDB; P16013; -.
DR   SMR; P16013; -.
DR   IntAct; P16013; 1.
DR   STRING; 3562.P16013; -.
DR   GeneID; 2715597; -.
DR   KEGG; soe:2715597; -.
DR   OrthoDB; 826802at2759; -.
DR   Proteomes; UP000054095; 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; Electron transport; Heme; Iron; Membrane;
KW   Metal-binding; Photosynthesis; Plastid; Reference proteome; Signal;
KW   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..320
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023837"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         36
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:0000250"
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
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:0000250"
FT   CONFLICT        235
FT                   /note="G -> R (in Ref. 1; AAA84632)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35319 MW;  33B9FE0D02F19C36 CRC64;
     MQTINTFSWI KEQITRSISI SLILYIITRS SIANAYPIFA QQGYENPREA TGRIVCANCH
     LANKPVDIEV PQAVLPDTVF EAVVRIPYDM QLKQVLANGK KGGLNVGAVL ILPEGFELAP
     PDRISPEMKE KMGNLSFQSY RPNKQNILVI GPVPGQKYSE ITFPILAPDP ATKKDVHFLK
     YPIYVGGNRG RGQIYPDGSK SNNTVYNSTA TGIVKKIVRK EKGGYEINIA DASDGREVVD
     IIPRGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEVVL QDPLRIQGLL FFFASVILAQ
     IFLVLKKKQF EKVQLSEMNF