CYF_SOYBN
ID CYF_SOYBN Reviewed; 320 AA.
AC P49161; Q2PMS1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Glycine max (Soybean) (Glycine hispida).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Resnik; TISSUE=Leaf;
RA Reverdatto S.V., Beilinson V., Nielsen N.C.;
RT "The rps16, accD, psaI, ORF 203, ORF 151, ORF 103, ORF 229 and petA gene
RT cluster in the chloroplast genome of soybean.";
RL (er) Plant Gene Register PGR95-051(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI 437654;
RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0;
RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G.,
RA Jansen R.K.;
RT "Complete chloroplast genome sequence of Glycine max and comparative
RT analyses with other legume genomes.";
RL Plant Mol. Biol. 59:309-322(2005).
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; U26948; AAA80649.1; -; Genomic_DNA.
DR EMBL; DQ317523; ABC25137.1; -; Genomic_DNA.
DR PIR; T06347; T06347.
DR RefSeq; YP_538777.1; NC_007942.1.
DR AlphaFoldDB; P49161; -.
DR SMR; P49161; -.
DR STRING; 3847.GLYMA12G36150.1; -.
DR PRIDE; P49161; -.
DR ProMEX; P49161; -.
DR EnsemblPlants; KRH27390; KRH27390; GLYMA_12G232900.
DR GeneID; 3989309; -.
DR Gramene; KRH27390; KRH27390; GLYMA_12G232900.
DR KEGG; gmx:3989309; -.
DR eggNOG; ENOG502QPT8; Eukaryota.
DR InParanoid; P49161; -.
DR OMA; FWAQQNY; -.
DR OrthoDB; 826802at2759; -.
DR Proteomes; UP000008827; Chloroplast.
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; Reference proteome; Signal; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000250"
FT CHAIN 36..320
FT /note="Cytochrome f"
FT /id="PRO_0000023836"
FT TRANSMEM 286..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 36
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 56
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 /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 60
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 320 AA; 35322 MW; 4013848FBE160E51 CRC64;
MQTRNAFSCI KEGITRSISI SIMIYIIIRA PISNAYPIFA QQGYENPREA TGRIVCANCH
LANKPVDIEV PQAVLPDTVF EAVVRIPYDM QVKQVLANGK KGALNVGAVL ILPEGFELAP
PDRISPEIKE KIGNLSFQNY RPTKKNILVV GPVPGQKYKE ITFPILSPDP TTKRDVHFLK
YPIYVGGNRG RGQIYLDGSK SNNNVYNATA AGMVKKIIRK EKGGYEITIV DALDGREVID
IIPPGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFFASIILAQ
IFLVLKKKQF EKVQLSEMNF
