ID   Q46ZM2_CUPPJ            Unreviewed;       950 AA.
AC   Q46ZM2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Reut_A2047 {ECO:0000313|EMBL:AAZ61411.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ61411.1};
RN   [1] {ECO:0000313|EMBL:AAZ61411.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ61411.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000090; AAZ61411.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46ZM2; -.
DR   STRING; 264198.Reut_A2047; -.
DR   KEGG; reu:Reut_A2047; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   OrthoDB; 9759785at2; -.
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: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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAZ61411.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          597..794
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   950 AA;  106010 MW;  52F026DBED7DB5EF CRC64;
     MMQQYQSNSY LFGGNAPYVE ELYEAYLQNP TSVPDNWRAY FDAMQNVPAV DGSNSRDVPH
     APIVASFAER AKAGPIKTIV ASADSDMGRK RVAATQLIAA YRNIGSHWAD LDPLKRQERP
     PLPDLDPAFY GFSEADLDIV FNASNTYFGK ESMSLRELLN NLRETYCGTI GAEFMYVSDQ
     AQKRWWQERL ESTRSKPVFT LEKKKHILDR LTAAEGLERF LHTKYVGQKR FSLEGGESFI
     AAMDELIQEA GSKGVQEIVI GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK
     YHKGFSSDVS TQGGPVHLSL AFNPSHLEIV NPVVEGSSKA RQERRGDAGH KEVLPVQVHG
     DAAFAGQGVV METLNLAQTR GYGTGGSMHI VINNQIGFTT SDPRDARSTL YCTDVVKMIE
     APVLHVNGDD PEAVVYAMQL AVDFRMEFNK DVVVDIICFR KLGHNEQDTP AVTQPLMYKK
     ISQHPGTRKL YADKLVAQNL VPADFGDQKV KEYRAAMDAG KHTSDPVLSN FKNKFAVDWM
     PFLNRKWTDA ADTAVPVTEL KRLAERITTT PETLKLHPLV EKVVKDRANM GRGDQPLDWG
     MGEHLAFASL VASGYPVRIT GQDAGRGTFT HRHAVLHDQA RERWDAGSYV PLQNVSENQA
     PFTVIDSVLS EEAVLGFEYG YSAAEPNAMV IWEAQFGDFV NGAQVVIDQF ISSGEVKWGR
     ASGLTLMLPH GYEGQGPEHS SARIERFLQL CADHNMQVCQ PTTPAQIFHL LRRQMIRLFR
     KPLVIMTPKS LLRNKDAVSP LSDLAKGHFE TVIPDHEELN ASKVKRVIMC SGKVYYDLVN
     TRKEREANDT AIIRVEQLYP FPHKALATEL KKYPNANEIL WCQDEPQNQG AWFFVQHYIM
     ENMTEGQKLG YAGRPASASP AVGYYAKHNE QQKALLDAAF SKLKGFVLTK
//