ID   ODO1_GEOSW              Reviewed;         952 AA.
AC   C5D802;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
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};
GN   OrderedLocusNames=GWCH70_0919;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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:0000255|HAMAP-Rule:MF_01169}.
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:0000255|HAMAP-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; CP001638; ACS23783.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5D802; -.
DR   SMR; C5D802; -.
DR   STRING; 471223.GWCH70_0919; -.
DR   KEGG; gwc:GWCH70_0919; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OrthoDB; 9759785at2; -.
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   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   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
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   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; Thiamine pyrophosphate.
FT   CHAIN           1..952
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_1000213736"
SQ   SEQUENCE   952 AA;  108481 MW;  D00671DCFA511D3B CRC64;
     MTKQTMNYAE PWSQFYGPNL GYVMEMYEQY LEDPDSVDPE LKQLFKEWGA PTTEAERFDH
     SESAAKTYQT FRLPENPTIF SKLVAAVKLA DKIRHYGHLA ADINPLNTQN KDTRRIELSE
     FDLTEDDLKQ IPVAFICPHA PAHVKNGLDA INHLRKIYTD KIAFEFSQVH NLEERNWLIS
     QIESGAYYPS LTNEEKVALL RRLTEVEGFE KFLHRTFVGQ KRFSIEGLDS MVPLLDELIR
     HSIEEEVKAV NIGMAHRGRL NVLAHVLGKP YEMIFAEFQH AESKDFMPSE GSVAITYGWT
     GDVKYHLGAA RRLRNKNEHT MRITLANNPS HLEVVNPVVL GFTRAAQEDR SNAGVPSQDT
     DSAFAIMIHG DAAFPGQGIV AETLNLSRLQ GYQTGGSIHI IANNMIGFTT ESYDSRSTKY
     ASDIAKGFEI PIVHVNADDP EACLAAANLA FAYRKRFKKD FVIDLIGYRR FGHNEMDEPM
     ATNPTMYSII QQHPTVRQLY AQKLIEKGII TKEAVEEMER EVAERLKIAY EKVPKDESKL
     DFIMDPPKPV ASKLPFVKTS VEKDVLRRLN KELLQFPSDF HVFNKLERIL KRREGVFDGK
     GKIDWAHAEI LAFATILRDG VPIRLTGQDS QRGTFAQRHL VLHDMKTGEE FVPLHHISDA
     NASFVVYNSP LTEAAVLGYE YGYNVFAPET LVLWEAQFGD FANMAQVMFD QFISSGRAKW
     GQKSGLVMLL PHGYEGQGPE HSSGRLERFL QLAAENNWTV ANLSTAAQYF HILRRQAGIL
     QREEVRPLVL MTPKSLLRHP LAASDVEEFT NGQFHPVIEQ KGLGENREKV ERIILCTGKF
     AIDLAEQINK MEGLDWLHIV RVEELYPFPK EELQAIFARY PNVKEIIWAQ EEPKNMGSWC
     YVEPKLREIA PDEVDVSYIG RRRRASPAEG DPVVHRKEQE RIIQCALTKK EQ
//