ID   ODO1_ALKHC              Reviewed;         945 AA.
AC   Q9KAT1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=BH2206;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05925.1; -; Genomic_DNA.
DR   PIR; F83925; F83925.
DR   RefSeq; WP_010898362.1; NC_002570.2.
DR   AlphaFoldDB; Q9KAT1; -.
DR   SMR; Q9KAT1; -.
DR   STRING; 272558.10174825; -.
DR   EnsemblBacteria; BAB05925; BAB05925; BAB05925.
DR   KEGG; bha:BH2206; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   Proteomes; UP000001258; 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..945
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162165"
SQ   SEQUENCE   945 AA;  106970 MW;  DF3D694B15EEAA5C CRC64;
     MSSKEHTSEE PWQGFYGPNL GVAVELYEEY QKDPNAVDDE LREAFEKWGP PPATAPERTQ
     STFTAASITD PDVIKKFVGA VKLADHIRAF GHLAADIQPI LKEQRREDMF DLDRFGLTES
     DIRSVPVDLL CPYAPAHVKN GLDAINHLKE VYTKTIAFEF VHVTDEEERK WLNRMIESGL
     YLPNLSTEQR KSLLKRLTDV EGFEKFLHRT FVGQKRFSIE GLDTLVPMLD EVVREAVHEG
     TTNVMIGMAH RGRLNVLAHV LNKPYEMIFA EFLHSLNKDL FPSEGSIGIN YGWTGDVKYH
     LGADRQIRDE NTAEARLTLA NNPSHLEFVS PIVEGYARAA QEDRTSPGAP EQDIMKAYSI
     LIHGDAAFPG QGVVTETLNL SRLTGYQTGG SLHIIANNNI GFTTETFDSR STLYSSDPAK
     GFEIPIVHVN ADDPEACLAA VHLAFQYRKR FKKDFLIDLI GYRRFGHNEM DEPAVTQPGV
     YQIIRKHPTV RELYSKQLVK KGLIDEQTVK QLDDEVQDKL QSVYEETLRN RTDEHLPDTP
     PVEVVNGLPK LDTGVQSETL KAINNELLEW PESFSVNPKL EKILKRRLNV FDGDGKVDWA
     LAETLAFATI LHDGTPIRLT GQDSERGTFA HRHLVLHDSR TNDVHSPLQS FRHANASFAV
     HNSPLSEMAI VGFEYGYNVF APETLVLWEA QFGDFANGAQ VMFDQWVSAG RAKWGQKSGL
     VCLLPHGYEG QGPEHSSARL ERFLVLAAEN NWTIANCTSA AQYFHILRRQ AAILNTDSVR
     PLIMMTPKSL LRNQKVASSV EELTTGRFKT VLEQPNLGES HEKVERIVLC SGKIAIDLQD
     RIEKEADKDW DWVHIVRVEQ LYPFPKEPLQ EIFARYPNVK EIVWSQEEPR NMGAWPFVQS
     KIRRAAPNGI NVRYEGRTYR SSPAEGDPII HKQEQERIVT ETLTR