VORB_PYRFU
ID VORB_PYRFU Reviewed; 311 AA.
AC Q51802;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ketoisovalerate oxidoreductase subunit VorB;
DE Short=VOR;
DE EC=1.2.7.7;
DE AltName: Full=2-oxoisovalerate ferredoxin reductase subunit beta;
DE AltName: Full=2-oxoisovalerate oxidoreductase beta chain;
GN Name=vorB; OrderedLocusNames=PF0968;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8550425; DOI=10.1128/jb.178.1.248-257.1996;
RA Kletzin A., Adams M.W.W.;
RT "Molecular and phylogenetic characterization of pyruvate and 2-
RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and
RT pyruvate ferredoxin oxidoreductase from Thermotoga maritima.";
RL J. Bacteriol. 178:248-257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + CoA + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = 2-methylpropanoyl-CoA + CO2 + H(+) + 2 reduced [2Fe-
CC 2S]-[ferredoxin]; Xref=Rhea:RHEA:11712, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57338; EC=1.2.7.7;
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain.
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DR EMBL; X85250; CAA59503.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81092.1; -; Genomic_DNA.
DR PIR; T45086; T45086.
DR RefSeq; WP_011012105.1; NC_018092.1.
DR AlphaFoldDB; Q51802; -.
DR SMR; Q51802; -.
DR STRING; 186497.PF0968; -.
DR EnsemblBacteria; AAL81092; AAL81092; PF0968.
DR GeneID; 41712780; -.
DR KEGG; pfu:PF0968; -.
DR PATRIC; fig|186497.12.peg.1027; -.
DR eggNOG; arCOG01601; Archaea.
DR HOGENOM; CLU_058423_0_0_2; -.
DR OMA; PCILEIG; -.
DR OrthoDB; 29720at2157; -.
DR PhylomeDB; Q51802; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Oxidoreductase; Reference proteome.
FT CHAIN 1..311
FT /note="Ketoisovalerate oxidoreductase subunit VorB"
FT /id="PRO_0000099957"
SQ SEQUENCE 311 AA; 34766 MW; 07CC02452E3C6074 CRC64;
MEVPENIKKR VTIPFEEHFY AGHTACQGCG ASLGLRYVLK AYGKKTILVI PACCSTIIAG
PWPYSAIDAN LFHTAFETTG AVISGIEAAL KAMGYKVKGE DGIMVVGWAG DGGTADIGLQ
ALSGFLERGH DAVYIMYDNE AYMNTGIQRS SSTPYGAWTT NTPGGRRHFL EKRHKKKVID
IVIAHRIPYA ATASIAYPED FIRKLKKAQK ISGPSFIQLF APCPTGWRAP TDKSIEIARL
AVQTAYFPLF EYENGKYKIN MPNPKKEPKP IEEFLKLQGR FKYMTKEDIE TLQKWVLEEW
ERLKKLAEVF G
