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}; 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
//
