ID   VORB_METTM              Reviewed;         352 AA.
AC   P80908; D9PWT7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   02-SEP-2026, entry version 96.
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=MTBMA_c10910;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanobacteria; Methanobacteriales; Methanobacteriaceae;
OC   Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-36, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=9108258; DOI=10.1111/j.1432-1033.1997.00862.x;
RA   Tersteegen A., Linder D., Thauer R.K., Hedderich R.;
RT   "Structures and functions of four anabolic 2-oxoacid oxidoreductases in
RT   Methanobacterium thermoautotrophicum.";
RL   Eur. J. Biochem. 244:862-868(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + 2 oxidized [2Fe-2S]-[ferredoxin] +
CC         CoA = 2-methylpropanoyl-CoA + 2 reduced [2Fe-2S]-[ferredoxin] + CO2 +
CC         H(+); Xref=Rhea:RHEA:11712, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57338; EC=1.2.7.7;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.7. {ECO:0000269|PubMed:9108258};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.
CC         {ECO:0000269|PubMed:9108258};
CC   -!- SUBUNIT: Heterotrimer of the VorA, VorB and VorC subunits.
CC       {ECO:0000269|PubMed:9108258}.
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DR   EMBL; CP001710; ADL58685.1; -; Genomic_DNA.
DR   RefSeq; WP_013295908.1; NC_014408.1.
DR   AlphaFoldDB; P80908; -.
DR   SMR; P80908; -.
DR   STRING; 79929.MTBMA_c10910; -.
DR   PaxDb; 79929-MTBMA_c10910; -.
DR   GeneID; 77399867; -.
DR   GeneID; 9704799; -.
DR   KEGG; mmg:MTBMA_c10910; -.
DR   PATRIC; fig|79929.8.peg.1069; -.
DR   HOGENOM; CLU_017038_0_0_2; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR052368; 2-oxoacid_oxidoreductase.
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   NCBIfam; NF005507; PRK07119.1; 1.
DR   PANTHER; PTHR43088:SF1; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43088; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9108258"
FT   CHAIN           2..352
FT                   /note="Ketoisovalerate oxidoreductase subunit VorB"
FT                   /id="PRO_0000099955"
SQ   SEQUENCE   352 AA;  38549 MW;  6BFE2D51CA971021 CRC64;
     MATQMVKGNT AVIIGAMYAG CDCYFGYPIT PASEILHEAS RYFPLVGRKF VQAESEEAAI
     NMVYGAAAAG HRVMTASSGP GMSLKQEGIS FLAGAELPAV IVDVMRAGPG LGNIGPEQAD
     YNQLVKGGGH GNYRNIVLAP NSVQEMCDLT MDAFELADKY RNPVIILADA VLGQMAEPLR
     FPERAVEHRP DTSWAVCGSR ETMKNLVTSI FLDFDELEEF NFYLQEKYAA VEENEVRYEE
     YMVEDAEIVL VAYGISSRVA KSAVDTARAD GIKVGLLRPI TLFPFPSERI RELAEGGCTF
     ISVEMSSGQM REDIKMASGC RDVELVNRMG GNLIELRDIL RKIREIAGES ND
//