ID ODO1_BACCQ Reviewed; 955 AA.
AC B9IU58;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=BCQ_1324;
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM11754.1; -; Genomic_DNA.
DR AlphaFoldDB; B9IU58; -.
DR SMR; B9IU58; -.
DR KEGG; bcq:BCQ_1324; -.
DR HOGENOM; CLU_004709_1_0_9; -.
DR Proteomes; UP000000441; 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 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; Thiamine pyrophosphate.
FT CHAIN 1..955
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_1000164359"
SQ SEQUENCE 955 AA; 106498 MW; 8E52C6E86A05BD83 CRC64;
MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP SFQDDVVTGD
NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM EDAANGQSLL EKAMNELSDA
DLKAIPAKTV WQDAPEGIHT ALDVIHRLKE VYTQTLAYEF SHIQDSEERA WLHQMVESNS
LRQPLSNQKR TALLKRLTAV EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG
VEDVMIGMAH RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV
SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPEQDTSKSF VILVHGDAAF
PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD SRSTKYSSDL AKGFDIPIVH
VNADDPEACL AAANLAIQYR MLFKKDFLID LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP
TVRAIYADQL QAAGVLNADE IETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG
IQSIDTGVEL 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
EYNLDEIHIV RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA
GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVSHALDVK YNFRQDKLEI EVFSN
//
