CYF_SYNPW
ID CYF_SYNPW Reviewed; 310 AA.
AC A5GMW2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE Flags: Precursor;
GN Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
GN OrderedLocusNames=SynWH7803_1851;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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:0000255|HAMAP-Rule:MF_00610}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00610};
CC Note=Binds 1 heme group covalently. {ECO:0000255|HAMAP-Rule:MF_00610};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00610}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00610}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00610}.
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000255|HAMAP-
CC Rule:MF_00610}.
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DR EMBL; CT971583; CAK24277.1; -; Genomic_DNA.
DR RefSeq; WP_011933749.1; NC_009481.1.
DR AlphaFoldDB; A5GMW2; -.
DR SMR; A5GMW2; -.
DR STRING; 32051.SynWH7803_1851; -.
DR EnsemblBacteria; CAK24277; CAK24277; SynWH7803_1851.
DR KEGG; syx:SynWH7803_1851; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_033498_0_0_3; -.
DR OMA; FWAQQNY; -.
DR OrthoDB; 744890at2; -.
DR Proteomes; UP000001566; Chromosome.
DR GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR GO; GO:0031676; C:plasma membrane-derived 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; 2.60.40.830; -; 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 Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW Reference proteome; Signal; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT CHAIN 28..310
FT /note="Cytochrome f"
FT /id="PRO_0000342042"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT BINDING 28
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:0000255|HAMAP-Rule:MF_00610"
FT BINDING 48
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT BINDING 51
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT BINDING 52
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:0000255|HAMAP-Rule:MF_00610"
SQ SEQUENCE 310 AA; 32876 MW; CC11EF54E0012F7E CRC64;
MRRLLSPLFA ALIVGVTVLT APSTSWAYPF WAQQNYDSPR EATGKIVCAN CHLAQKLTQA
EVPQSVLPDS VFKAVVKIPY DTSVPEIGAD GSEVPLQVGA VVMLPDGFTL APQDRWTDDI
KEETEGVYFS EYSDDQPNVI LVGPIPGDQH QEIVFPVLSP DPATDSNIHF GKYSIHVGGN
RGRGQVYPTG EKSNNTVFTA PSTGTVRSIE AGENGASVVT IASADGTELS ETVPVGPALI
VSVGDAVEAG APITNDPNVG GFGQLDTEVV LQNPVRIYGL LAFFAAVALA QIMLVLKKKQ
FEKVQAAEGV
