VORA_PYRFU
ID VORA_PYRFU Reviewed; 394 AA.
AC Q51801;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PF0969;
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 1-22.
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; CAA59502.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81093.1; -; Genomic_DNA.
DR PIR; T45085; T45085.
DR RefSeq; WP_011012106.1; NC_018092.1.
DR AlphaFoldDB; Q51801; -.
DR SMR; Q51801; -.
DR IntAct; Q51801; 1.
DR STRING; 186497.PF0969; -.
DR PRIDE; Q51801; -.
DR EnsemblBacteria; AAL81093; AAL81093; PF0969.
DR GeneID; 41712781; -.
DR KEGG; pfu:PF0969; -.
DR PATRIC; fig|186497.12.peg.1028; -.
DR eggNOG; arCOG01608; Archaea.
DR HOGENOM; CLU_002569_5_0_2; -.
DR OMA; MKSNYIS; -.
DR OrthoDB; 29908at2157; -.
DR PhylomeDB; Q51801; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW Direct protein sequencing; Oxidoreductase; Reference proteome.
FT CHAIN 1..394
FT /note="Ketoisovalerate oxidoreductase subunit VorA"
FT /id="PRO_0000099952"
SQ SEQUENCE 394 AA; 43960 MW; D8E580E790CEBB2B CRC64;
MEYKPIRKVV SGNYAAAYAA LHARVQVVAA YPITPQTSII EKIAEFIANG EADIQYIPVE
SEHSAMAACI GASATGARTF TATSAQGLAL MHEMLHWAAG ARLPIVMVDV NRAMAPPWSV
WDDQTDSLSQ RDTGWMQFYA ENNQEVYDGV LMAYKVAETV NVPAMVVESA FILSHTYDVV
EMIPQELVDE FLPPRKPLYS LANFDEPIAV GALATPNDYY EFRYKLAKAH EEAKKVIKEV
GKEFGERFGR DYSQMIETGY IDDADFVFMG MGSLMGTVKE AVDLLRKEGY KVGYAKVRWF
RPFPKEELVE IAESVKGIAV LDRNFSFGQE GILFTESKGA LYNSSAHPLM KNYIVGLGGR
DVTVKDIKAI ADDMKKVIES GKVDKEVVWY HLKR