VORC_METTM
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 03-AUG-2022, entry version 91.
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; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; 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 + 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 -!- 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 EnsemblBacteria; ADL58684; ADL58684; MTBMA_c10900.
DR GeneID; 9704798; -.
DR KEGG; mmg:MTBMA_c10900; -.
DR PATRIC; fig|79929.8.peg.1068; -.
DR HOGENOM; CLU_139698_5_3_2; -.
DR OMA; NERGYHY; -.
DR OrthoDB; 124457at2157; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF12838; Fer4_7; 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; 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
