CYF_OENEH
ID CYF_OENEH Reviewed; 318 AA.
AC P04658; Q9MTK8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Oenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera
OS hookeri).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX NCBI_TaxID=85636;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3442826; DOI=10.1007/bf00419877;
RA Tyagi A.K., Herrmann R.G.;
RT "Location and nucleotide sequence of the pre-apocytochrome f gene on the
RT Oenothera hookeri plastid chromosome (Euoenothera plastome I).";
RL Curr. Genet. 10:481-486(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Johansen;
RX PubMed=10852478; DOI=10.1007/pl00008686;
RA Hupfer H., Swiatek M., Hornung S., Herrmann R.G., Maier R.M., Chiu W.-L.,
RA Sears B.;
RT "Complete nucleotide sequence of the Oenothera elata plastid chromosome,
RT representing plastome I of the five distinguishable Euoenothera
RT plastomes.";
RL Mol. Gen. Genet. 263:581-585(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83, AND MUTANT PM7.
RC STRAIN=cv. Johansen;
RX PubMed=2390787; DOI=10.1007/bf00313083;
RA Johnson E.M., Sears B.B.;
RT "Structure and expression of cytochrome f in an Oenothera plastome
RT mutant.";
RL Curr. Genet. 17:529-534(1990).
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; X03570; CAA27251.1; -; Genomic_DNA.
DR EMBL; AJ271079; CAB67170.1; -; Genomic_DNA.
DR EMBL; X55574; CAA39160.1; -; Genomic_DNA.
DR PIR; S00431; S00431.
DR RefSeq; NP_084705.1; NC_002693.2.
DR AlphaFoldDB; P04658; -.
DR SMR; P04658; -.
DR GeneID; 802732; -.
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 Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Plastid; Signal; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000250"
FT CHAIN 34..318
FT /note="Cytochrome f"
FT /id="PRO_0000023824"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 34
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 54
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 58
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 MUTAGEN 3
FT /note="N->NRN: In PM7."
FT CONFLICT 254
FT /note="I -> T (in Ref. 1; CAA27251)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> Q (in Ref. 1; CAA27251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 34928 MW; 4EDAAD56032E8F92 CRC64;
MKNTFSWIKK EITRSISLSL MIYIITRTSI SNAYPIFAQQ GYENPREATG RIVCANCHLA
NKPVDIEVPQ AVLPDTVFEA VVRIPYDRQV KQVLANGKKG GLNVGAVLIL PEGFELAPPA
RISPEMKERI GNPSFQSYRP TKKNILVIGP VPGQKYSEIT FPILSPDPAT NKDVHFLKYP
IYVGGNRGRG QIYPDGSKSN NTVYNATAAG IVSKIIRKEK GGYEITITDA SDGRQVVDII
PSGPELLVSE GESIKLDQPL TSNPNVGGFG QGDAEVVLQD PLRVQGLLFF LASVILAQIF
LVLKKKQFEK VQLSEMNF
