VORB_PYRAB
ID VORB_PYRAB Reviewed; 311 AA.
AC Q9UYZ2; G8ZHH1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=PYRAB13650; ORFNames=PAB1473;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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. {ECO:0000250}.
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DR EMBL; AJ248287; CAB50270.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70808.1; -; Genomic_DNA.
DR PIR; A75047; A75047.
DR RefSeq; WP_010868480.1; NC_000868.1.
DR AlphaFoldDB; Q9UYZ2; -.
DR SMR; Q9UYZ2; -.
DR STRING; 272844.PAB1473; -.
DR EnsemblBacteria; CAB50270; CAB50270; PAB1473.
DR GeneID; 1496754; -.
DR KEGG; pab:PAB1473; -.
DR PATRIC; fig|272844.11.peg.1451; -.
DR eggNOG; arCOG01601; Archaea.
DR HOGENOM; CLU_058423_0_0_2; -.
DR OMA; PCILEIG; -.
DR OrthoDB; 29720at2157; -.
DR PhylomeDB; Q9UYZ2; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW Oxidoreductase.
FT CHAIN 1..311
FT /note="Ketoisovalerate oxidoreductase subunit VorB"
FT /id="PRO_0000099956"
SQ SEQUENCE 311 AA; 34759 MW; 1EBE2609519DAC30 CRC64;
MEVPEDVKRR LTLPFEENFF AGHTACQGCG ASLGLRYVLK AYGRKTILVI PACCSTIIAG
PWPYSALNAN LFHTAFETTG AVISGIEAAL KALGYKVKGE DGIMVVGWAG DGGTADIGLQ
ALSGFLERGH DALYIMYDNE AYMNTGIQRS SSTPYGAWTT NTPGGKRHFL EKRHKKKVID
IVIAHRIPYA ATASVAYPED FLRKLKKAQK IPGPSFIQLF APCPTGWRAP TDKTIEIARL
AVQTAYFPLF EYENGKYKIN MPNPKKEPKP IEEFLKLQGR FKYMTKEDIE VLQKWVLEEW
ERLKKLAEVF G
