ID   KORB_METTM              Reviewed;         285 AA.
AC   P80905; D9PXQ5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=2-oxoglutarate synthase subunit KorB;
DE            EC=1.2.7.3;
DE   AltName: Full=2-ketoglutarate oxidoreductase beta chain;
DE            Short=KOR;
DE   AltName: Full=2-oxoglutarate-ferredoxin oxidoreductase subunit beta;
GN   Name=korB; OrderedLocusNames=MTBMA_c14160;
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 1-21, 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=2-oxoglutarate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2
CC         + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + succinyl-CoA;
CC         Xref=Rhea:RHEA:17297, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292; EC=1.2.7.3;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9. {ECO:0000269|PubMed:9108258};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:9108258};
CC   -!- SUBUNIT: Heterotetramer of the KorA, KorB, KorC and KorD subunits.
CC       {ECO:0000269|PubMed:9108258}.
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DR   EMBL; CP001710; ADL59003.1; -; Genomic_DNA.
DR   RefSeq; WP_013296215.1; NC_014408.1.
DR   AlphaFoldDB; P80905; -.
DR   SMR; P80905; -.
DR   STRING; 79929.MTBMA_c14160; -.
DR   EnsemblBacteria; ADL59003; ADL59003; MTBMA_c14160.
DR   GeneID; 9705125; -.
DR   KEGG; mmg:MTBMA_c14160; -.
DR   PATRIC; fig|79929.8.peg.1380; -.
DR   HOGENOM; CLU_048564_2_0_2; -.
DR   OMA; SAWIASP; -.
DR   OrthoDB; 43666at2157; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0047553; F:2-oxoglutarate synthase 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   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase.
FT   CHAIN           1..285
FT                   /note="2-oxoglutarate synthase subunit KorB"
FT                   /id="PRO_0000099944"
SQ   SEQUENCE   285 AA;  31121 MW;  AF2F28C7EA2DBC95 CRC64;
     MNVKENPYLK YLRRDRLPHI FCAGCGNGIV LNTFFKGMEM AGVDFDSIAM VSGIGCSSRI
     PGYVKCDSLH TTHGRPIAFA TGLKLANPSL NVVVFTGDGD AAAIGGNHLI HGARKNIDLT
     VICINNSIYG MTGGQISPTS PEGSFGTTAP YGALEDPFDL SELVRAAGAS YVARWTAAHP
     LQLANSIKKG LKNRGFSFIE AVSQCPTYFG RKNRMRSPVE MMKFMKENSI NRRKALKMDP
     EEVEGKLIIG EFADAPRPEL CDRIYGMIEE KSGKIDIIKS AYRDD