CYF_PEA
ID CYF_PEA Reviewed; 320 AA.
AC P00155;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6319031; DOI=10.1016/0092-8674(84)90248-4;
RA Willey D.L., Auffret A.D., Gray J.C.;
RT "Structure and topology of cytochrome f in pea chloroplast membranes.";
RL Cell 36:555-562(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
RC STRAIN=cv. Alaska;
RX PubMed=1807835; DOI=10.1007/bf00317074;
RA Nagano Y., Matsuno R., Sasaki Y.;
RT "Sequence and transcriptional analysis of the gene cluster trnQ-zfpA-psaI-
RT ORF231-petA in pea chloroplasts.";
RL Curr. Genet. 20:431-436(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=2103453; DOI=10.1007/bf00036920;
RA Willey D.L., Gray J.C.;
RT "An open reading frame encoding a putative haem-binding polypeptide is
RT cotranscribed with the pea chloroplast gene for apocytochrome f.";
RL Plant Mol. Biol. 15:347-356(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-320.
RC TISSUE=Shoot;
RX PubMed=2766383; DOI=10.1007/bf00435508;
RA Willey D.L., Gray J.C.;
RT "Two small open reading frames are co-transcribed with the pea chloroplast
RT genes for the polypeptides of cytochrome b-559.";
RL Curr. Genet. 15:213-220(1989).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85363.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA39759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; K01516; AAA85363.1; ALT_INIT; Genomic_DNA.
DR EMBL; X56315; CAA39759.1; ALT_INIT; Genomic_DNA.
DR EMBL; X53525; CAA37603.1; -; Genomic_DNA.
DR EMBL; X15767; CAA33776.1; -; Genomic_DNA.
DR PIR; A00148; CFPM.
DR RefSeq; YP_003587555.1; NC_014057.1.
DR AlphaFoldDB; P00155; -.
DR SMR; P00155; -.
DR PRIDE; P00155; -.
DR GeneID; 9073103; -.
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; Signal; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000250"
FT CHAIN 36..320
FT /note="Cytochrome f"
FT /id="PRO_0000023828"
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; 35148 MW; 70E21E21E4A11106 CRC64;
MQTRNAFSWI KKEITRSISV LLMIYIITRA PISNAYPIFA QQGYENPREA TGRIVCANCH
LANKPVDIEV PQAVLPDTVF EAVVRIPYDM QVKQVLANGK KGALNVGAVL ILPEGFELAP
PHRLSPQIKE KIGNLSFQSY RPTKKNILVI GPVPGKKYSE ITFPILSPDP ATKRDVYFLK
YPLYVGGNRG RGQIYPDGSK SNNNVSNATA TGVVKQIIRK EKGGYEITIV DASDGSEVID
IIPPGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL LFLASIILAQ
ILLVLKKKQF EKVQLSEMNF
