ODO1_CUPNH
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 25-MAY-2022, entry version 127.
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; Proteobacteria; 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 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=(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;
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 PRIDE; Q59106; -.
DR EnsemblBacteria; CAJ93421; CAJ93421; H16_A2325.
DR GeneID; 57644455; -.
DR KEGG; reh:H16_A2325; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_4; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 29166at2; -.
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 Gene3D; 3.40.50.11610; -; 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 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_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
