CYF_SOLLC
ID CYF_SOLLC Reviewed; 320 AA.
AC Q2MI87;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE Flags: Precursor;
GN Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. LA3023;
RX PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA Tomkins J., Jansen R.K.;
RT "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT lycopersicum and comparative analyses with other Solanaceae genomes.";
RL Theor. Appl. Genet. 112:1503-1518(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. IPA-6;
RX PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT solanaceous plastid genomes.";
RL J. Mol. Evol. 63:194-207(2006).
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:0000255|HAMAP-Rule:MF_00610}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00610};
CC Note=Binds 1 heme group covalently. {ECO:0000255|HAMAP-Rule:MF_00610};
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:0000255|HAMAP-Rule:MF_00610}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00610}.
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000255|HAMAP-
CC Rule:MF_00610}.
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DR EMBL; DQ347959; ABC56313.1; -; Genomic_DNA.
DR EMBL; AM087200; CAJ32406.1; -; Genomic_DNA.
DR RefSeq; AP_004941.1; AC_000188.1.
DR RefSeq; XP_004228573.1; XM_004228525.3.
DR RefSeq; YP_008563101.1; NC_007898.3.
DR AlphaFoldDB; Q2MI87; -.
DR SMR; Q2MI87; -.
DR STRING; 4081.Solyc01g007380.1.1; -.
DR PaxDb; Q2MI87; -.
DR PRIDE; Q2MI87; -.
DR GeneID; 3950466; -.
DR KEGG; sly:3950466; -.
DR eggNOG; ENOG502QPT8; Eukaryota.
DR HOGENOM; CLU_033498_0_0_1; -.
DR InParanoid; Q2MI87; -.
DR OrthoDB; 826802at2759; -.
DR PhylomeDB; Q2MI87; -.
DR Proteomes; UP000004994; Chloroplast.
DR ExpressionAtlas; Q2MI87; baseline and differential.
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:0000255|HAMAP-Rule:MF_00610"
FT CHAIN 36..320
FT /note="Cytochrome f"
FT /id="PRO_0000275451"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
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:0000255|HAMAP-Rule:MF_00610"
FT BINDING 56
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT BINDING 59
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
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:0000255|HAMAP-Rule:MF_00610"
SQ SEQUENCE 320 AA; 35218 MW; 6053D37CD5A84097 CRC64;
MQTRNAFSWL KKQITRSISV SLMIYILTRT SISSAYPIFA QQGYENPREA TGRIVCANCH
LANKPVEIEV PQAVLPDTVF EAVVRIPYDM QLKQVLANGK KGGLNVGAVL ILPEGFELAP
PDRISPEMKE KIGNLSFQSY RPNKTNILVV GPVPGKKYSE ITFPILSPDP ATKKDVHFLK
YPIYVGGNRG RGQIYPDGNK SNNTVYNATA AGIVSKIIRK EKGGYEITIT DASEGRQVVD
IIPPGPELLV SEGESIKFDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFLASVILAQ
IFLVLKKKQF EKVQLAEMNF
