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VORB_PYRHO
ID   VORB_PYRHO              Reviewed;         311 AA.
AC   O58414;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
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=PH0681;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA29772.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000001; BAA29772.1; ALT_INIT; Genomic_DNA.
DR   PIR; B71114; B71114.
DR   RefSeq; WP_048053190.1; NC_000961.1.
DR   AlphaFoldDB; O58414; -.
DR   SMR; O58414; -.
DR   STRING; 70601.3257089; -.
DR   EnsemblBacteria; BAA29772; BAA29772; BAA29772.
DR   GeneID; 1443009; -.
DR   KEGG; pho:PH0681; -.
DR   eggNOG; arCOG01601; Archaea.
DR   OMA; EYAIPTP; -.
DR   OrthoDB; 29720at2157; -.
DR   Proteomes; UP000000752; 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_0000099958"
SQ   SEQUENCE   311 AA;  34569 MW;  E27B65877EF65813 CRC64;
     MEIPEEVKKR LTIPFEENFF AGHTACQGCG ASLGLRYVLK AYGRKTIVVI PACCSTIIAG
     PWPYSALNAN LFHTAFATTG AVISGIEAGL KALGYKVKGE DGIMVVGWAG DGGTADIGLQ
     ALSGFIERGH DAVYIMYDNE AYMNTGIQRS SSTPYGAWTT NTPGGKRHLL EKRHKKKVID
     IVIAHRIPYA ATASVAYPED FIRKLKKAQK IPGPSFIQLF APCPTGWRAP TDKSIEIARL
     AVQTAYFPLF EYENGKYKIN MPNPKKEPKP IEEFLKLQGR FKYMTKEDVE ALQKWVLEEW
     ERLKKLAEVF G
 
 
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