CYB_RHOCA
ID CYB_RHOCA Reviewed; 437 AA.
AC P0CY47; P07057; P08502;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Cytochrome b;
GN Name=petB; Synonyms=cytB;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GA;
RX PubMed=3004982; DOI=10.1111/j.1432-1033.1986.tb09437.x;
RA Gabellini N., Sebald W.;
RT "Nucleotide sequence and transcription of the fbc operon from
RT Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid
RT sequences of the FeS protein, cytochrome b and cytochrome c1.";
RL Eur. J. Biochem. 154:569-579(1986).
RN [2]
RP SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3004982 ORIGINATES FROM RHODOBACTER
RP CAPSULATUS.
RX PubMed=2821272; DOI=10.1016/0022-2836(87)90324-x;
RA Davidson E., Daldal F.;
RT "fbc operon, encoding the Rieske Fe-S protein cytochrome b, and cytochrome
RT c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is
RT from Rhodopseudomonas capsulata.";
RL J. Mol. Biol. 195:25-29(1987).
RN [3]
RP MUTATIONS CONFERRING RESISTANCE TO QUINOL OXIDATION INHIBITORS.
RX PubMed=2556259; DOI=10.1002/j.1460-2075.1989.tb08578.x;
RA Daldal F., Tokito M.K., Davidson E., Faham M.;
RT "Mutations conferring resistance to quinol oxidation (Qz) inhibitors of the
RT cyt bc1 complex of Rhodobacter capsulatus.";
RL EMBO J. 8:3951-3961(1989).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 2 heme b groups non-covalently. {ECO:0000250};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC at about 566 nm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
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DR EMBL; X03476; CAA27195.1; -; Genomic_DNA.
DR PIR; B29336; B29336.
DR PDB; 1ZRT; X-ray; 3.50 A; C/P=1-437.
DR PDBsum; 1ZRT; -.
DR AlphaFoldDB; P0CY47; -.
DR SMR; P0CY47; -.
DR TCDB; 3.D.3.1.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR EvolutionaryTrace; P0CY47; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00290; cytochrome_b_C; 1.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR030689; Cytochrome_b.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF038885; COB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..437
FT /note="Cytochrome b"
FT /id="PRO_0000061772"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 111
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 198
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 212
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 47..66
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 90..117
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 188..219
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 247..269
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 329..349
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 361..380
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 407..415
FT /evidence="ECO:0007829|PDB:1ZRT"
SQ SEQUENCE 437 AA; 49324 MW; 65E756D2F55EDE5B CRC64;
MSGIPHDHYE PKTGIEKWLH DRLPIVGLVY DTIMIPTPKN LNWWWIWGIV LAFTLVLQIV
TGIVLAIDYT PHVDLAFASV EHIMRDVNGG WAMRYIHANG ASLFFLAVYI HIFRGLYYGS
YKAPREITWI VGMVIYLLMM GTAFMGYVLP WGQMSFWGAT VITGLFGAIP GIGPSIQAWL
LGGPAVDNAT LNRFFSLHYL LPFVIAALVA IHIWAFHTTG NNNPTGVEVR RTSKADAEKD
TLPFWPYFVI KDLFALALVL LGFFAVVAYM PNYLGHPDNY IQANPLSTPA HIVPEWYFLP
FYAILRAFAA DVWVVILVDG LTFGIVDAKF FGVIAMFGAI AVMALAPWLD TSKVRSGAYR
PKFRMWFWFL VLDFVVLTWV GAMPTEYPYD WISLIASTYW FAYFLVILPL LGATEKPEPI
PASIEEDFNS HYGNPAE
