CYF_SYNY3
ID CYF_SYNY3 Reviewed; 328 AA.
AC P26287;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA; OrderedLocusNames=sll1317;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1907512; DOI=10.1007/bf00039508;
RA Mayes S.R., Barber J.;
RT "Primary structure of the psbN-psbH-petC-petA gene cluster of the
RT cyanobacterium Synechocystis PCC 6803.";
RL Plant Mol. Biol. 17:289-293(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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: Cellular thylakoid membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR EMBL; X58532; CAA41423.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17627.1; -; Genomic_DNA.
DR PIR; S16573; S16573.
DR AlphaFoldDB; P26287; -.
DR SMR; P26287; -.
DR IntAct; P26287; 10.
DR STRING; 1148.1652707; -.
DR TCDB; 3.D.3.5.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P26287; -.
DR EnsemblBacteria; BAA17627; BAA17627; BAA17627.
DR KEGG; syn:sll1317; -.
DR eggNOG; COG3258; Bacteria.
DR InParanoid; P26287; -.
DR OMA; FWAQQNY; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0009512; C:cytochrome b6f complex; IDA:UniProtKB.
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..44
FT /evidence="ECO:0000250"
FT CHAIN 45..328
FT /note="Cytochrome f"
FT /id="PRO_0000023848"
FT TRANSMEM 296..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 45
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 66
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 70
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 328 AA; 35231 MW; 6ABBEE56697D86AB CRC64;
MRNPDTLGLW TKTMVALRRF TVLAIATVSV FLITDLGLPQ AASAYPFWAQ ETAPLTPREA
TGRIVCANCH LAQKAAEVEI PQAVLPDTVF EAVVKIPYDL DSQQVLGDGS KGGLNVGAVL
MLPEGFKIAP PDRLSEGLKE KVGGTYFQPY REDMENVVIV GPLPGEQYQE IVFPVLSPDP
AKDKSINYGK FAVHLGANRG RGQIYPTGLL SNNNAFKAPN AGTISEVNAL EAGGYQLILT
TADGTETVDI PAGPELIVSA GQTVEAGEFL TNNPNVGGFG QKDTEVVLQN PTRIKFLVLF
LAGIMLSQIL LVLKKKQIEK VQAAELNF
