CYF_CUCSA
ID CYF_CUCSA Reviewed; 320 AA.
AC Q2QD76; A5J1U7; Q4VZH9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE Flags: Precursor;
GN Name=petA {ECO:0000255|HAMAP-Rule:MF_00610}; OrderedLocusNames=CsCp053;
OS Cucumis sativus (Cucumber).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekmibaekdadagi;
RX PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA Choi D.-W., Liu J.R., Cho K.Y.;
RT "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT Baekmibaekdadagi) chloroplast genome.";
RL Plant Cell Rep. 25:334-340(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Borszczagowski;
RX PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT genome: its composition and comparative analysis.";
RL Cell. Mol. Biol. Lett. 12:584-594(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chipper, and cv. Gy14;
RX PubMed=17546086; DOI=10.1139/g07-003;
RA Chung S.-M., Gordon V.S., Staub J.E.;
RT "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT differences between chilling-tolerant and -susceptible cucumber lines.";
RL Genome 50:215-225(2007).
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; DQ119058; AAZ94664.1; -; Genomic_DNA.
DR EMBL; AJ970307; CAJ00771.1; -; Genomic_DNA.
DR EMBL; DQ865975; ABI97430.1; -; Genomic_DNA.
DR EMBL; DQ865976; ABI98758.1; -; Genomic_DNA.
DR RefSeq; YP_247612.1; NC_007144.1.
DR AlphaFoldDB; Q2QD76; -.
DR SMR; Q2QD76; -.
DR GeneID; 3429265; -.
DR KEGG; csv:3429265; -.
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:0000255|HAMAP-Rule:MF_00610"
FT CHAIN 36..320
FT /note="Cytochrome f"
FT /id="PRO_0000275407"
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"
FT CONFLICT 70
FT /note="V -> G (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="VV -> GG (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="G -> W (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="V -> G (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 132..139
FT /note="MGNLSFQS -> KGQSVLFRA (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="I -> F (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="Q -> H (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..317
FT /note="QLSE -> NCPK (in Ref. 2; CAJ00771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35157 MW; 812D9F4419AD2B56 CRC64;
MQTRNTFSSI KEEITRSISV SLMIYIITWA PVSNAYPIFA QQGYENPREA TGRIVCANCH
LANKPVDIEV PQAVLPDTVF EAVVRIPYDM QLKQVLANGK KGGLNVGAVL ILPEGFELAP
PDRISPEIKE KMGNLSFQSY RPTKKNILVI GPVPGQKYSE ITFPILSPDP ATKKDVHFLK
YPIYVGGNRG RGQIYPDGSK SNNNVYNATA AGIVSKIIRK EKGGYEITIV DAANGRQVVD
IIPPGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFFASVILAQ
IFLVLKKKQF EKVQLSEMNF
