CYF_DESSP
ID CYF_DESSP Reviewed; 333 AA.
AC P13626;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Desmonostoc sp. (strain PCC 7906) (Nostoc sp. (strain PCC 7906)).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Desmonostoc.
OX NCBI_TaxID=1181;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2842748; DOI=10.1073/pnas.85.16.5794;
RA Kallas T., Spiller S., Malkin R.;
RT "Primary structure of cotranscribed genes encoding the Rieske Fe-S and
RT cytochrome f proteins of the cyanobacterium Nostoc PCC 7906.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5794-5798(1988).
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; J03855; AAA23333.1; -; Genomic_DNA.
DR AlphaFoldDB; P13626; -.
DR SMR; P13626; -.
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 Signal; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..44
FT CHAIN 45..333
FT /note="Cytochrome f"
FT /id="PRO_0000023844"
FT TRANSMEM 301..318
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 333 AA; 35931 MW; 683F4A74AF557F77 CRC64;
MRNASVTARL TRSVRAIVKT LLIAIATVTF YFSCDLALPQ SAAAYPFWAQ QTYPETPREP
TGRIVCANCH LAAKPTEVEV PQSVLPDTVF KAVVKIPYDT SAQQVGADGS KVGLNVGAVL
MLPEGFKIAP EDRISEELQE EIGDTYFQPY SEDKENIVIV GPLPGEQYQE IVFPVLSPNP
ATDKNIHFGK YSVHVGGNRG RGQVYPTGEK SNNNLYNASA TGTIAKIAKE EDEDGNVKYQ
VNIQPESGDV VVDTVPAGPE LIVSEGQAVK AGDALTNNPN VGGFGQRDAE IVLQDAGRVK
GLIAFVALVM LAQVMLVLKK KQVERVQAAE MNF