ID   CYF_PICAB               Reviewed;         319 AA.
AC   O47042;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA;
OS   Picea abies (Norway spruce) (Picea excelsa).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Philipps A., Sutter A., Wild A.;
RT   "PetA from Picea abies.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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; AJ001023; CAA04479.1; -; Genomic_DNA.
DR   PIR; T14833; T14833.
DR   AlphaFoldDB; O47042; -.
DR   SMR; O47042; -.
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   3: Inferred from homology;
KW   Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Plastid; Signal; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..319
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023830"
FT   TRANSMEM        285..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         35
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         55
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                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
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"
SQ   SEQUENCE   319 AA;  35151 MW;  E137A1AFCD258F90 CRC64;
     MQNRNTYDLK KKMTRLISVL VMIHIITRTS ISNAYPIFAQ QGYENPREAT GRIVCANCHL
     AKKPVDIEGP QSVLPNTVFE AVVKIPYDTQ MKQVLANGKK GALNVGAVLI LPEGFELAPP
     DRISPEIRQK MGNLYFQNYR PNQKNIIVIG PVPGQKYSEL VFPILSPDPA TDKEAHFLKY
     PIYLGGNRGR GQIYPDGSKS NNTVYSASAT GRVSKILRKE KGGYEITIDN TSDGGQVVDI
     VPPGPELLIS EGELIKVDQP LTNNPNVGGF GQGDAEIVLQ DPLRVKGLLL FLASVILAQI
     FLVLKKKQFE KVQLAEMNL