ID   ODO1_CUPNH              Reviewed;         950 AA.
AC   Q59106; Q0K9A0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=H16_A2325;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8867378; DOI=10.1111/j.1574-6968.1996.tb08054.x;
RA   Hein S., Steinbuechel A.;
RT   "Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate
RT   dehydrogenase complex.";
RL   FEMS Microbiol. Lett. 136:231-238(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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:0000250|UniProtKB:P0AFG3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P0AFG3};
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:0000250|UniProtKB:P0AFG3}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X91877; CAA62980.1; -; Genomic_DNA.
DR   EMBL; AM260479; CAJ93421.1; -; Genomic_DNA.
DR   PIR; T44422; T44422.
DR   RefSeq; WP_010809464.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q59106; -.
DR   SMR; Q59106; -.
DR   STRING; 381666.H16_A2325; -.
DR   GeneID; 57644455; -.
DR   KEGG; reh:H16_A2325; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
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   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
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_0000162160"
FT   CONFLICT        621
FT                   /note="G -> A (in Ref. 1; CAA62980)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   950 AA;  105996 MW;  531BC77561D2ECCF CRC64;
     MMQQYQSNSY LFGGNAPYVE ELYEAYLQNP ASVPDNWRAY FDAMQNVPAV DGSNGRDIPH
     APIVASFAER AKQGPIRTIV ASADSDMGRK RVAATQLIAA YRNIGSHWAD LDPLKRQERP
     PLPDLDPAFY GFSEADLDIV FNASNTYFGK ESMSLRELLN NLRETYCGTI GFEFMYVSDQ
     AQKRWWQERL ETTRSKPVFT LEKKKHILDR LTAAEGLERF LHTKYVGQKR FSLEGGESFI
     AAMDELIQHA GSKGVQEIVI GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK
     YHKGFSSDVS TEGGPVHLSL AFNPSHLEIV NPVVEGSAKA RQERRGEVGH KEVLPVQVHG
     DAAFAGQGVV METLNLAQTR GYGTGGSMHI VINNQIGFTT SDPRDARSTL YCTDVVKMIE
     APVLHVNGDD PEAVVYAMQL AVDFRMEFKK DVVVDIICFR KLGHNEQDTP AVTQPLMYKK
     IAQHPGTRKL YADKLAAQNL VPAEFGDEKV KAYRAAMDAG KHTADPVLSN FKNKFAVDWM
     PFLNRKWTDA ADTAVPVTEL KRLAERITTT PETLKLHPLV EKVVKDRANM GRGDQPLDWG
     MGEHLAFASL VSSGYPVRIT GQDAGRGTFT HRHAVLHDQA RERWDAGSYV PLQNVSENQA
     PFTVIDSVLS EEAVLGFEYG YSAAEPNALV IWEAQFGDFV NGAQVVIDQF ISSGEVKWGR
     ASGLTLMLPH GYEGQGPEHS SARIERFLQL CADHNMQVCQ PTTPAQIFHL LRRQMIRLFR
     KPLVIMTPKS LLRNKDAVSP LSDLAKGHFE TVIPDHEELN ASKVKRVIMC SGKVYYDLVN
     TRKEREANDT AVIRLEQLYP FPHKAVAAEL KKYPNATEIV WCQDEPQNQG AWFFVQHYIM
     ENMTDGQKLG YAGRPASASP AVGYYAKHNE QQKALLEAAF AKLKGFVLTK
//