ID   A0A1B1UQE0_9BRAD        Unreviewed;       985 AA.
AC   A0A1B1UQE0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   ORFNames=LMTR13_37650 {ECO:0000313|EMBL:ANW05009.1};
OS   Bradyrhizobium icense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1274631 {ECO:0000313|EMBL:ANW05009.1, ECO:0000313|Proteomes:UP000092839};
RN   [1] {ECO:0000313|EMBL:ANW05009.1, ECO:0000313|Proteomes:UP000092839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMTR 13 {ECO:0000313|EMBL:ANW05009.1,
RC   ECO:0000313|Proteomes:UP000092839};
RA   Ormeno-Orrillo E., Duran D., Rogel M.A., Rey L., Imperial J.,
RA   Ruiz-Argueso T., Martinez-Romero E.;
RT   "Complete genome sequence of Bradyrhizobium icense LMTR 13T, a potential
RT   inoculant strain isolated from lima bean (Phaseolus lunatus) in Peru.";
RL   Submitted (JUL-2016) 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};
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:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP016428; ANW05009.1; -; Genomic_DNA.
DR   RefSeq; WP_065732144.1; NZ_CP016428.1.
DR   AlphaFoldDB; A0A1B1UQE0; -.
DR   STRING; 1274631.LMTR13_37650; -.
DR   KEGG; bic:LMTR13_37650; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000092839; Chromosome.
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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          632..825
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   985 AA;  110837 MW;  6479B0A1948CF2DC CRC64;
     MSRQDANAAF ALSSFLQGTN ATYIDELYSR YEQNPGSVDS DWQEFFKSLK DTPADVQKNA
     DGPSWGRDNW PITPQDELTS ALDGNWVTVE KAVGAKLAAK AQAKGAELSP ADVNQATRDS
     VRALMLIRAY RMRGHFHAKL DPLGIEAPRD REELDPRTYG FTEADFDRKI FLDHVLGLEY
     GTLREIVAIC ERTYCQTLGV EFMHISNAAQ KAWIQERIEG PDKEISFTRE GRRAILNKLI
     EAEGFEKFCD LKFTGTKRFG LDGAESLIPA LEQIIKRGGN LGVKEIVLGM PHRGRLNVLT
     QVMGKSHRAL FHEFKGGSAN PEDVEGSGDV KYHLGASSDR EFDGNKIHLS LTANPSHLEI
     VDPVVLGKVR AKQDQHGDPP DMRISVLPLL LHGDAAFAGQ GVVAECFGLS DLKGYRTGGS
     LHFIVNNQIG FTTYPRYSRS SPYPSDVAKM IDAPIFHVNG DDPEAVVFAA KVAIEFRQKF
     HKPVVIDMFC YRRHGHNEGD EPGFTQPVMY KRIASHPSTL ALYAKRLVAD GVLTEGEVDK
     AKADWRARLD AELEAGAGYK PNKADWLDGK WAGFKVADQE EDARRGVTGV DVSILKDIGR
     KITKVPDGFR VHRTIQRYLE NRAKAIDNGV GIDWATGEAL AICTLLQEGH HVRLSGQDSE
     RGTFSQRHSV LIDQEDESRY TPFNHLGHEQ GHYEVINSLL SEEAVLGFEY GYSLAEPNAL
     AMWEAQFGDF ANGAQVVFDQ FISSGERKWL RMSGLVCLLP HGYEGQGPEH SSARLERYLQ
     MCAEDNMQVV YPTTPANYFH VLRRQLHREI RKPLIMMTPK SLLRHKRAIS QLDELGKDTT
     FHRILYDDAQ MLPDEKIKLA PDDKIRRVVL CSGKVYYDLY EEREKRDIDD IYLLRVEQLY
     PVPLKALVHE LARFKNAEVV WCQEEPRNMG AWHFIEPYLE WVLNQIHAPN RRPRYAGRAA
     SAATATGLMS KHLAQLKAML DEALN
//