ID   ODO1_BACCR              Reviewed;         955 AA.
AC   Q81GF2;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=BC_1252;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08237.1; -; Genomic_DNA.
DR   RefSeq; NP_831036.1; NC_004722.1.
DR   RefSeq; WP_000197160.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81GF2; -.
DR   SMR; Q81GF2; -.
DR   STRING; 226900.BC_1252; -.
DR   KEGG; bce:BC1252; -.
DR   PATRIC; fig|226900.8.peg.1225; -.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
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; IBA:GO_Central.
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   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   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; 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; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..955
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162163"
SQ   SEQUENCE   955 AA;  106412 MW;  99F267C26CA28433 CRC64;
     MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP SFQDDVVTGD
     NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM EDAANGQSLL EKAMSELSDA
     DLKAIPAKTV WQDAPEGIHT ALDVIHRLKD VYTKSLAYEF SHIQDSEERA WLHQMVESNS
     LRQPLSNKKR TALLKRLTAV EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG
     VEDVMIGMAH RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV
     SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPDQDTSKSF VILVHGDAAF
     PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD SRSTKYSSDL AKGFDIPIVH
     VNADDPEACL AAANLAIQYR MLFKKDFLID LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP
     TVRAIYADQL QAAGVLNADE VETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG
     IQPIDTGVEI DSLRAINEGL LSWPEGFNVY PKVKKILERR KDALEENGKI EWALAESLAF
     ASILQEGTPI RLTGQDSQRG TFAHRHIVLH DTDTNETYSP LHRLPNINAS FSVHNSPLSE
     AAVVGYEYGY NVFAPETLVM WEAQYGDFSN TAQALFDQYV SAGRAKWGQK SGLVLLLPHG
     YEGQGPEHSS ARPERFLQLA AENNWTVANL TSAAQYFHIL RRQASILGTE AVRPLVLMTP
     KSLLRHPLTL STASQLSEGR FQPALEQENL GMKPNKVKRL VLSTGKMAID LAAEIESGKH
     EYNLDEVHVV RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA
     GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVAHALDVK YNFRQDKQEI EVYSN
//