ID   ODO1_OCEIH              Reviewed;         953 AA.
AC   Q8CUL8;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=OB1089;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13045.1; -; Genomic_DNA.
DR   RefSeq; WP_011065490.1; NC_004193.1.
DR   AlphaFoldDB; Q8CUL8; -.
DR   SMR; Q8CUL8; -.
DR   STRING; 221109.22776770; -.
DR   PRIDE; Q8CUL8; -.
DR   EnsemblBacteria; BAC13045; BAC13045; BAC13045.
DR   KEGG; oih:OB1089; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   PhylomeDB; Q8CUL8; -.
DR   Proteomes; UP000000822; 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; 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; 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..953
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162175"
SQ   SEQUENCE   953 AA;  107266 MW;  78AB32B7CFBE7A6E CRC64;
     MAENAESAER FWGQFHGQNT GYLEQQFELY KEDPELVESS IRTIFDTHGA PSWLSSTENV
     KSVSNASDFD VTKLTSAIRL VEAIRRYGHT DADIYPVGGY KGDRSKMLDL STYNLKEQDL
     EKIPASWIWE KQAPGVATAL DVVNQLKKYY TGTITFEYDH VNNDEERKWL FDLIEEGNAR
     LDPSDDERKK ILQRLADVEG FEKFLHKTFV GQKRFSIEGL ESMVPMIDHI VQYSNQDSIE
     HVMMGMAHRG RLSVLANVLG KPYDKIFSEF NYTKEKELMP SEGSRAINYG WTGDVKYHYG
     AEKEVEFGNK GQTRITLAHN PSHLEFVNPV VEGFTRAAQD DRSEKGYPKQ VTNKAVSVLI
     HGDAAFIGEG VVAETLNLSG LPGYSTGGTL HIIANNLLGY TTDREDGRST RYASDLAKGF
     EIPVIRVNAD DPISCISAIK IAYEYRQKFQ KDFLIDLVGY RRYGHNEMDE PRTTQPSLYQ
     QIDDHPSVAS LFGKGMEEKG ILQEGGFEEV KSAVEKKLTD IYKGMTESEI GEPEAKLMPQ
     VLTNGLDQFT TAIDLATLKS INEELLERPE GFKGFKKTER ILQRRKDALE EGNKADWGTG
     EALAFASILK EGTPIRLTGQ DTERGTFAHR HIVLHDVETG EKYSPLHGLS DVEASFDVRN
     SPLSEAGVLG FEYGYSVQSP DTLVIWEAQF GDFANAGQVI FDQFISSARA KWGEKSNMVL
     LLPHGYEGQG PEHSSARLER FLQMAAENNW IVANVTSSAQ LFHILRRQAA MRDRDEARPL
     VLMTPKSSLI RHPRMGATAE EFTDGGFLAL RDQPGFEANR EKVTRLVVGS GKMMIDIEEA
     MDDSDETYDW LQIKRVEQIY PFPKKALEEE IKQLPNLKEI VWVQEEPKNM GAWNFVDDYL
     RELLNEDQKL KVISRPDRSA PAGGIPTVHK TAQNKIIKQA LNQSEGGKSS AGN