CYF_PHOLA
ID CYF_PHOLA Reviewed; 338 AA.
AC P95522;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Phormidium laminosum.
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=32059;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8856106; DOI=10.1016/0005-2728(96)00084-9;
RA Wagner M.J., Packer J.C.L., Howe C.J., Bendall D.S.;
RT "Some characteristics of cytochrome f in the cyanobacterium Phormidium
RT laminosum: its sequence and charge properties in the reaction with
RT plastocyanin.";
RL Biochim. Biophys. Acta 1276:246-252(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 46-295, AND COFACTOR.
RX PubMed=10423236; DOI=10.1021/bi9903190;
RA Carrell C.J., Schlarb B.G., Bendall D.S., Howe C.J., Cramer W.A.,
RA Smith J.L.;
RT "Structure of the soluble domain of cytochrome f from the cyanobacterium
RT Phormidium laminosum.";
RL Biochemistry 38:9590-9599(1999).
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;
CC Evidence={ECO:0000269|PubMed:10423236};
CC Note=Binds 1 heme group covalently. {ECO:0000269|PubMed:10423236};
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; Y09612; CAA70824.1; -; Genomic_DNA.
DR PDB; 1CI3; X-ray; 1.90 A; M=46-294.
DR PDBsum; 1CI3; -.
DR AlphaFoldDB; P95522; -.
DR SMR; P95522; -.
DR EvolutionaryTrace; P95522; -.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Signal; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..45
FT CHAIN 46..338
FT /note="Cytochrome f"
FT /id="PRO_0000023845"
FT TRANSMEM 300..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 46
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:0000269|PubMed:10423236"
FT BINDING 66
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:10423236"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:10423236"
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:0000269|PubMed:10423236"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1CI3"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1CI3"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1CI3"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1CI3"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1CI3"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:1CI3"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1CI3"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 189..201
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1CI3"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:1CI3"
SQ SEQUENCE 338 AA; 36069 MW; BD3D52036181FB50 CRC64;
MNFKVCSFPS RRQSIAAFVR VLMVILLTLG ALVSSDVLLP QPAAAYPFWA QQNYANPREA
TGRIVCANCH LAAKPAEIEV PQAVLPDSVF KAVVKIPYDH SVQQVQADGS KGPLNVGAVL
MLPEGFTIAP EDRIPEEMKE EVGPSYLFQP YADDKQNIVL VGPLPGDQYE EIVFPVLSPN
PATNKSVAFG KYSIHLGANR GRGQIYPTGE KSNNAVYNAS AAGVITAIAK ADDGSAEVKI
RTEDGTTIVD KIPAGPELIV SEGEEVAAGA ALTNNPNVGG FGQKDTEIVL QSPNRVKGRI
AFLAAITLTQ ILLVLKKKQV ERVQAGRDDL LKAAFIAG
