ID   ODO1_GEOKA              Reviewed;         950 AA.
AC   Q5L172;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=odhA {ECO:0000255|HAMAP-Rule:MF_01169}; OrderedLocusNames=GK1023;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC         COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000255|HAMAP-
CC       Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR   EMBL; BA000043; BAD75308.1; -; Genomic_DNA.
DR   RefSeq; WP_011230523.1; NC_006510.1.
DR   AlphaFoldDB; Q5L172; -.
DR   SMR; Q5L172; -.
DR   STRING; 235909.GK1023; -.
DR   PRIDE; Q5L172; -.
DR   EnsemblBacteria; BAD75308; BAD75308; GK1023.
DR   KEGG; gka:GK1023; -.
DR   PATRIC; fig|235909.7.peg.1118; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OMA; RDSYCRT; -.
DR   Proteomes; UP000001172; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.50.11610; -; 1.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..950
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162172"
SQ   SEQUENCE   950 AA;  107561 MW;  0A9769B6BB8BC10F CRC64;
     MAKQTNYAQP WSQFYGPNLG YVIEMYEQYL DDPNSIDPEL KQLFEQWGAP VLEEPVSPAD
     DETAKTHQTF RLPETPTIFS KLVAAVKLAD SIRHYGHLVA DTNPLVKKEK KLRRLELDEY
     DLTEEDLKRI PVAFLCPHAP AHVKNGWDAI LHLRKIYTDK IAFEFSQVHN LEERNWLIQQ
     IESGAYYPSL ANKERVALLR RLTEVEGFEK FIHRTYVGQK RFSIEGLDSM VPLLDELVRQ
     AIEHEIDAVN IGMAHRGRLN VLAHVLGKPY EMIFAEFQHA ESKNFIPSEG SVAITYGWTG
     DVKYHLGAAR RLRNQSAHTM RITLANNPSH LEVVNPVVLG YTRAAQEDRT KPGVPVQNTD
     ASFAILIHGD AAFPGQGIVA ETLNLSQLRG YTTGGTIHII ANNMIGFTTE SYDSRSTTYA
     SDMAKGFEVP IVHVNADDPE ACLAAACLAF AYRQRFKKDF VIDLIGYRRF GHNEMDEPMA
     TNPTMYAIIN QHPTVRKLYA QKLMEKGIIT EREVDEMEQE VAERLKIAYE RVPKNEDELD
     FIMDPPKPVV DRLPEVKTSV AKDVLHRVNE ELLQFPDGFN VFNKLERILK RRSGVFAQNG
     KVDWAHAEIL AFATILQDGV PIRLTGQDSQ RGTFAQRHLV LHDVKTGEEY VPLHHISGAK
     ASFVVYNSPL TEAAVLGYEY GYNVYAPETL VLWEAQFGDF ANMAQVMFDQ FISSGRAKWG
     QKSGLVMLLP HGYEGQGPEH SSGRVERFLQ LAAENNWTVA NLSTAAQYFH ILRRQAALLT
     REEVRPLIIM TPKSLLRHPL AASDAEVFVD GAFSPVLEQP GLGADAGKVE RIVFGTGKLM
     IDLAEQIGKM ESLDWLHIVR IEELYPFPEE AVKDIIARYP NVKELVWVQE EPKNMGAWLY
     MEPRLRALAP EGVDVSYIGR RRRASPAEGD PVVHRKEQER IIRCALTKHE