UCRI_ALLVD
ID UCRI_ALLVD Reviewed; 207 AA.
AC O31214; D3RUZ1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
DE EC=7.1.1.8;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=RISP;
GN Name=petA; OrderedLocusNames=Alvin_0068;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADC61040.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF034104; AAB86973.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC61040.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; O31214; -.
DR SMR; O31214; -.
DR STRING; 572477.Alvin_0068; -.
DR EnsemblBacteria; ADC61040; ADC61040; Alvin_0068.
DR KEGG; alv:Alvin_0068; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_055690_0_2_6; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR InterPro; IPR019470; Ubiq_cytC_Rdtase_Fe-S_su_TAT.
DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF10399; UCR_Fe-S_N; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Cell membrane; Disulfide bond; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..207
FT /note="Ubiquinol-cytochrome c reductase iron-sulfur
FT subunit"
FT /id="PRO_0000127760"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 100..199
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 134
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 162
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 165
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 139..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 80
FT /note="K -> M (in Ref. 1; AAB86973)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="P -> S (in Ref. 1; AAB86973)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="D -> G (in Ref. 1; AAB86973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 22190 MW; D88DCEDF24A74D33 CRC64;
MLASAGGYWP MSAQGVNKMR RRVLVAATSV VGAVGAGYAL VPFVASMNPS ARARAAGAPV
EADISKLEPG ALLRVKWRGK PVWVVHRSPE MLAALSSNDP KLVDPTSEVP QQPDYCKNPT
RSIKPEYLVA IGICTHLGCS PTYRPEFGPD DLGSDWKGGF HCPCHGSRFD LAARVFKNVP
APTNLVIPKH VYLNDTTILI GEDRGSA
