ID   VORC_METTM              Reviewed;          79 AA.
AC   P80909; D9PWT6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   02-SEP-2026, entry version 100.
DE   RecName: Full=Ketoisovalerate oxidoreductase subunit VorC;
DE            Short=VOR;
DE            EC=1.2.7.7;
DE   AltName: Full=2-oxoisovalerate ferredoxin reductase subunit gamma;
DE   AltName: Full=2-oxoisovalerate oxidoreductase gamma chain;
GN   Name=vorC; OrderedLocusNames=MTBMA_c10900;
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 1-24, 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
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; ADL58684.1; -; Genomic_DNA.
DR   RefSeq; WP_013295907.1; NC_014408.1.
DR   AlphaFoldDB; P80909; -.
DR   SMR; P80909; -.
DR   STRING; 79929.MTBMA_c10900; -.
DR   PaxDb; 79929-MTBMA_c10900; -.
DR   GeneID; 92393709; -.
DR   GeneID; 9704798; -.
DR   KEGG; mmg:MTBMA_c10900; -.
DR   PATRIC; fig|79929.8.peg.1068; -.
DR   HOGENOM; CLU_139698_5_3_2; -.
DR   OrthoDB; 23833at2157; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.20; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Reference proteome; Repeat; Transport.
FT   CHAIN           1..79
FT                   /note="Ketoisovalerate oxidoreductase subunit VorC"
FT                   /id="PRO_0000099960"
FT   DOMAIN          4..33
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          40..70
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         13
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         16
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         19
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         23
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         49
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         52
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         55
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         59
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        22..23
FT                   /note="AC -> QA (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   79 AA;  9060 MW;  4A61AECE99CCA595 CRC64;
     MKKAYPVINR VECKACERCI IACPRKVLYM SNKINERGYH YVEYRGEGCN GCGNCYYTCP
     EINAIEVHIE RCEDGDTDG
//