ID   ODO1_EXISA              Reviewed;         951 AA.
AC   C4L3W2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=EAT1b_2538;
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=360911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b;
RX   PubMed=21460088; DOI=10.1128/jb.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ71457.1; -; Genomic_DNA.
DR   RefSeq; WP_015881016.1; NC_012673.1.
DR   AlphaFoldDB; C4L3W2; -.
DR   SMR; C4L3W2; -.
DR   STRING; 360911.EAT1b_2538; -.
DR   KEGG; eat:EAT1b_2538; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000000716; Chromosome.
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..951
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_1000213735"
FT   REGION          906..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   951 AA;  106924 MW;  BB172AC8134ADA9C CRC64;
     MGESSNVHEK SQAFYGPNLG YIIELYEQYL EDPSSVDEET RRYFDEFGAP ETSTPTEVPV
     SGPSFDLEKV VSATRLINDI RAFGHKAADI YPLKDHPREQ ELFELSRYDL TEEDLKQIPA
     RLLSDDAPKP NASALELFRH LLDVYTGTVA IELRHLDDME EKKWIRRQVE QGALQQTFSK
     EEKIELFKRL AETELFESFL HKTYVGQKRF SIEGLDAMVP LLDAMVGGLI SSGSEHINIG
     MAHRGRLNVL AHVLGKPYEM IFAEFQHAPN KELIPSEGSI GINFGWSGDV KYHLGLDRKV
     VEQQKEVRLN LANNPSHLEF VGSVVEGYTR AAQDDRSEKG SAVQHDDLAA SILIHGDAAF
     PGQGIVAETL NMTNLTGYRT GGTVHVIANN TIGFTTDPND SRSTRYASDI AKGYEIPVFH
     VNADDPEACV AVAKLISEYR AKFHKDILVD LIGYRRYGHN EMDEPMNTNP VLYKAIKGHQ
     SVRHVYAARL EEEGVMTKDE KAQIEQKIEE ALKAARDLVP SEEEDADIVL PDAVHKGFPK
     VDTSVEREFL TQLNEELLNW PEGFGVFHKL QKVLDRRRDA FSEGGKIDWG HAETLAFASI
     LSDGTPVRLS GQDSERGTFA QRNIMLNDVE SGKKFSPLHE LSTAKASFSV YNSPLSEGSV
     LGFEYGYNVF AQDTLVLWEA QYGDFANSAQ VMFDQFISAG RAKWGQKSGL VMLLPHGYEG
     QGPEHSSARM ERYLTLAGEK NWTVANLSSA AQYFHILRRQ AEMLGKEEIR PMIIMTPKSL
     LRHPLATSPV EAFTEESFKP IVEQPGLGEN TEKVERLVFC TGKMAIDLAE AVGKSEESLD
     FLHIVRVEEI YPFPVREIRD VISRYPNARE IVWVQEEPKN MGAWTYIEPR LEAVTTNRLD
     VRYIGRRRRS SPAEGNPTAH KQEQARIIRE ALSRDVVSSG AGTSTYQKDR K
//