CYF_BRARR
ID CYF_BRARR Reviewed; 320 AA.
AC P36438;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Brassica rapa subsp. rapa (Turnip).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=51350;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-45 AND 285-287,
RP AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=cv. Snowball;
RX PubMed=8055917; DOI=10.1111/j.1432-1033.1994.tb19016.x;
RA Gray J.C., Rochford R.J., Packman L.C.;
RT "Proteolytic removal of the C-terminal transmembrane region of cytochrome f
RT during extraction from turnip and charlock leaves generates a water-soluble
RT monomeric form of the protein.";
RL Eur. J. Biochem. 223:481-488(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 36-285 IN COMPLEX WITH HEME, AND
RP COFACTOR.
RX PubMed=8081747; DOI=10.1016/s0969-2126(00)00012-5;
RA Martinez S.E., Huang D., Szczepaniak A., Cramer W.A., Smith J.L.;
RT "Crystal structure of chloroplast cytochrome f reveals a novel cytochrome
RT fold and unexpected heme ligation.";
RL Structure 2:95-105(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 36-285 IN COMPLEX WITH HEME, AND
RP COFACTOR.
RX PubMed=8762139; DOI=10.1002/pro.5560050610;
RA Martinez S.E., Huang D., Ponomarev M., Cramer W.A., Smith J.L.;
RT "The heme redox center of chloroplast cytochrome f is linked to a buried
RT five-water chain.";
RL Protein Sci. 5:1081-1092(1996).
RN [4]
RP STRUCTURE BY NMR OF 36-285 IN COMPLEX WITH HEME, AND COFACTOR.
RX PubMed=9551554; DOI=10.1016/s0969-2126(98)00035-5;
RA Ubbink M., Ejdebaeck M., Karlsson B.G., Bendall D.S.;
RT "The structure of the complex of plastocyanin and cytochrome f, determined
RT by paramagnetic NMR and restrained rigid-body molecular dynamics.";
RL Structure 6:323-335(1998).
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:8081747, ECO:0000269|PubMed:8762139,
CC ECO:0000269|PubMed:9551554};
CC Note=Binds 1 heme group covalently. {ECO:0000269|PubMed:8081747,
CC ECO:0000269|PubMed:8762139, ECO:0000269|PubMed:9551554};
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; Single-
CC pass membrane protein.
CC -!- PTM: Purified from leaves as a water-soluble monomeric protein with a
CC mass of 28.16 kDa, cleavage occurs after Gln-287 and separates the
CC heme-binding from the membrane. {ECO:0000269|PubMed:8055917}.
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR EMBL; X77011; CAA54307.1; -; Genomic_DNA.
DR PIR; S45661; S45661.
DR PDB; 1CTM; X-ray; 2.30 A; A=36-285.
DR PDB; 1HCZ; X-ray; 1.96 A; A=36-287.
DR PDB; 1TKW; NMR; -; B=36-287.
DR PDB; 2PCF; NMR; -; B=36-285.
DR PDBsum; 1CTM; -.
DR PDBsum; 1HCZ; -.
DR PDBsum; 1TKW; -.
DR PDBsum; 2PCF; -.
DR AlphaFoldDB; P36438; -.
DR SMR; P36438; -.
DR DIP; DIP-62N; -.
DR MINT; P36438; -.
DR EvolutionaryTrace; P36438; -.
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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Photosynthesis; Plastid; Signal;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:8055917"
FT CHAIN 36..320
FT /note="Cytochrome f"
FT /id="PRO_0000023806"
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:0000269|PubMed:8081747,
FT ECO:0000269|PubMed:8762139, ECO:0000269|PubMed:9551554"
FT BINDING 56
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8081747,
FT ECO:0000269|PubMed:8762139, ECO:0000269|PubMed:9551554"
FT BINDING 59
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8081747,
FT ECO:0000269|PubMed:8762139, ECO:0000269|PubMed:9551554"
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:0000269|PubMed:8081747,
FT ECO:0000269|PubMed:8762139, ECO:0000269|PubMed:9551554"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1HCZ"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1HCZ"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1HCZ"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1HCZ"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:1HCZ"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 180..190
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:1HCZ"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1HCZ"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:1HCZ"
SQ SEQUENCE 320 AA; 35389 MW; 466324C040C3E00F CRC64;
MQTRNTFSWI REEITRSISV SLMIYIITWA SISSAYPIFA QQNYENPREA TGRIVCANCH
LASKPVDIEV PQAVLPDTVF EAVVKIPYDM QLKQVLANGK KGALNVGAVL ILPEGFELAP
PDRISPEMKE KIGNLSFQNY RPNKKNILVI GPVPGQKYSE ITFPILAPDP ATNKDVHFLK
YPIYVGGNRG RGQIYPDGSK SNNTVYNATA GGIISKILRK EKGGYEITIV DASNERQVID
IIPRGLELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFLGSVVLAQ
IFLVLKKKQF EKVQLSEMNF
