CYB_ALLVD
ID CYB_ALLVD Reviewed; 414 AA.
AC O31215; D3RUZ2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome b;
GN Name=petB; OrderedLocusNames=Alvin_0069;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX DOI=10.1023/A:1006052408216;
RA Chen Y.L., Dincturk H.B., Qin H., Knaff D.B.;
RT "The pet operon, encoding the prosthetic group-containing subunits of the
RT cytochrome bc1 complex, of the purple sulfur bacterium Chromatium
RT vinosum.";
RL Photosyn. Res. 57:149-158(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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; AF034104; AAB86974.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC61041.1; -; Genomic_DNA.
DR RefSeq; WP_012969317.1; NC_013851.1.
DR AlphaFoldDB; O31215; -.
DR SMR; O31215; -.
DR STRING; 572477.Alvin_0069; -.
DR EnsemblBacteria; ADC61041; ADC61041; Alvin_0069.
DR KEGG; alv:Alvin_0069; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_3_0_6; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 262439at2; -.
DR Proteomes; UP000001441; Chromosome.
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; 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 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..414
FT /note="Cytochrome b"
FT /id="PRO_0000061770"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 91
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 105
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 192
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 206
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT CONFLICT 112
FT /note="W -> R (in Ref. 1; AAB86974)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..414
FT /note="VPERVTS -> FLRG (in Ref. 1; AAB86974)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 47246 MW; 9C8C67B6DB065D9A CRC64;
MSAEKTENLS WIDKRFPLSE TWRNHLSEYY APKNLNFWSF FGSLAILTLV IQIVTGVWLA
MSYKPDAGLA FASVEYIMRD VDWGWLIRYM HSTGASMFFI VIYLHMFRGL LWGSYRKPRE
LLWMIGVVIY LVMMATAFFG YLLPWGQMSY WGAQVIVNLF AAVPVVGEDL SVWVRGDFVI
SDATLNRFFA FHFLLPFLLA GLVFLHIVAL HHVGSNNPDG IEIKEGPKGN RWSDKAPADG
IPFHPYYTVK DLMGVVVFLA IFGYVMFFNP TMGGLFLEAP NFQPANPMQT PAHIAPVWYF
TPFYAMLRAV PPMYGSQFPG VVVMFAAILI LFVLPWLDRS PVKSMRYKGP IFKWATGIFV
VSFVALAWLG IQPASDFYTL LSQIFTVLYF AYFLLMPIYS SLDKTKPVPE RVTS
