ID   ODO1_BACCN              Reviewed;         958 AA.
AC   A7GMD4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Bcer98_0961;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC         COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000255|HAMAP-
CC         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; CP000764; ABS21292.1; -; Genomic_DNA.
DR   RefSeq; WP_011984045.1; NC_009674.1.
DR   AlphaFoldDB; A7GMD4; -.
DR   SMR; A7GMD4; -.
DR   STRING; 315749.Bcer98_0961; -.
DR   EnsemblBacteria; ABS21292; ABS21292; Bcer98_0961.
DR   GeneID; 56416549; -.
DR   KEGG; bcy:Bcer98_0961; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   Proteomes; UP000002300; 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   Gene3D; 3.40.50.11610; -; 1.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
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   PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN           1..958
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_1000085384"
SQ   SEQUENCE   958 AA;  107259 MW;  C3D676435F9C4694 CRC64;
     MTRKNTATNP WAKFHGPNLG YVIEQYDRYM TNEGSVDPEL QELFETFGAP TFQVDVVTGD
     NKETNFSPQS TGNIETILKA VQVVENIRSF GHLSAHINPM EEPHDGQSLI ETMMRELNDV
     DLKAIPAKTV WPDAPNDVHT ALDAIHRLKD VYTKSLAYEF SHIQDSEERT WLHQMVESNS
     LRQPLSNQKR TALLKRLTAV EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EMIAEGAKAG
     VEDVMIGMAH RGRLSVLAHV LEKPYSHMFA EFKHATIQSD DKTNHNAGWT GDVKYHLGRE
     QVVGNETVRT RVTLANNPSH LEFVNPVVEG YARAAQENRK KAGYPEQDSS KSFVILVHGD
     AAFPGQGIVS ETLNLSRLNA YQTGGTIHII ANNTIGFTTD SYDSRSTRYS SDLAKGFDIP
     IVHVNADDPE ACLAAANLAI QYRLRFKKDI LIDLIGYRRY GHNEMDDPAV TQPQVYKKIK
     NHPTVRAIYA EQLKAEGVLS SDEVETITQF TQEQLKAEYA QVPPADTSEA AIHVKVPDVV
     ARGIQPIDTG LPLETLRAIN EGLLSWPEGF NVYPKVKKIL ERRRTALDAD GKVEWALAES
     LAFASILQEG TPIRLTGQDS QRGTFAQRHI VLHDTETNET YSPLHRLPNI NASFSVHNSP
     LSEAAVVGFE YGYNVFAPET LVMWEAQYGD FANTAQALFD QYVSSGRAKW GQKSGLVLLL
     PHGYEGQGPE HSSARPERFL QLAAENNWTV ANLTSAAQYF HILRRQASIL GTEAVRPLVI
     MTPKSLLRHP LTASTGSELS EGCFQPALEQ EKLGTKPTKV KRLIFTTGKM AIDLAAEIES
     GKHEYNLDEL HIVRIEQLYP FPAEKVQSII KRFKNLEEII WVQEEPRNMG AWHYMAPILF
     ELAGDKLKTG YIGRPDRSSP SGGDPHAHKA EQELIIAHAL DTNYNFRQDK QEIEVYSN