ID VORA_PYRAB Reviewed; 395 AA. AC Q9UYZ1; G8ZHH2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 03-AUG-2022, entry version 111. DE RecName: Full=Ketoisovalerate oxidoreductase subunit VorA; DE Short=VOR; DE EC=1.2.7.7; DE AltName: Full=2-oxoisovalerate ferredoxin reductase subunit alpha; DE AltName: Full=2-oxoisovalerate oxidoreductase alpha chain; GN Name=vorA; OrderedLocusNames=PYRAB13660; ORFNames=PAB1472; 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ248287; CAB50271.1; -; Genomic_DNA. DR EMBL; HE613800; CCE70809.1; -; Genomic_DNA. DR PIR; B75047; B75047. DR AlphaFoldDB; Q9UYZ1; -. DR SMR; Q9UYZ1; -. DR STRING; 272844.PAB1472; -. DR PRIDE; Q9UYZ1; -. DR EnsemblBacteria; CAB50271; CAB50271; PAB1472. DR KEGG; pab:PAB1472; -. DR PATRIC; fig|272844.11.peg.1452; -. DR eggNOG; arCOG01608; Archaea. DR HOGENOM; CLU_002569_5_0_2; -. DR OMA; MKSNYIS; -. DR PhylomeDB; Q9UYZ1; -. 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: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 CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1. DR Gene3D; 3.40.50.920; -; 1. DR InterPro; IPR033412; PFOR_II. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF17147; PFOR_II; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 4: Predicted; KW Oxidoreductase. FT CHAIN 1..395 FT /note="Ketoisovalerate oxidoreductase subunit VorA" FT /id="PRO_0000099951" SQ SEQUENCE 395 AA; 44230 MW; DF760EDF08CB6823 CRC64; MVEYKPIKKV VSGNYAAAYA VLHARVQVVA AYPITPQTSI IEKIAEFIAN GEADIQYIPV ESEHSAMAAC IGASATGARV FTATSAQGLA LMHEMLHWAA GARLPIVMVD VNRAMAPPWS VWDDQTDSLS QRDTGWMQFY AENNQEVYDG VLMAFKVAET VNVPAMVVES AFILSHTYEI VNMIPQELVD EFLPPRKPLY SLADFENPIA VGALATPADY YEFRYKLARA HEEAKKVIKD VGREFGERFG RDYSEMIEKA YIDDADFVFM GMGSLMGTVK EAVELLRKQG YKVGYAKVRW FRPFPREELL EIAESVKGIA VLDRNFSFGQ EGILFTEAKG ALYNNGARPI MKNYIVGLGG RDFTVSDVKA IAEDMKKVIE SGKLDREVEW YHLKR //