ID ODO1_STAAU Reviewed; 932 AA. AC P0C601; Q7ASB7; Q7WRM3; Q7WRN1; Q7WRX0; Q7WZ40; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 60. 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}; OS Staphylococcus aureus. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FranceDuf, Glasgow3700, Glasgow3759, LIM1, LIM2, LIM3, RC LiverpoolAG, LLA, LLE, Michigan, New Jersey, Norway1018, PC1, PC3, RC Slovenia6096, SMH10501, SMH11888, SMH12248, SMH14017, SMH17487, RC SMH17608, SMH18000, SMH18034, SMH18037, SMH2, SMH8997, Southampton23, RC St. Luke, Sweden307, and Sweden309; RA Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P., RA Walsh T.R.; RT "Genetic analysis of seventeen genes in Staphylococcus aureus with reduced RT susceptibility to vancomycin (VRSA) and hetero-VRSA (hVRSA)."; RL Submitted (MAY-2003) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ564531; CAD92198.1; -; Genomic_DNA. DR EMBL; AJ564532; CAD92199.1; -; Genomic_DNA. DR EMBL; AJ564533; CAD92200.1; -; Genomic_DNA. DR EMBL; AJ564534; CAD92201.1; -; Genomic_DNA. DR EMBL; AJ564535; CAD92202.1; -; Genomic_DNA. DR EMBL; AJ564536; CAD92203.1; -; Genomic_DNA. DR EMBL; AJ564537; CAD92204.1; -; Genomic_DNA. DR EMBL; AJ564538; CAD92205.1; -; Genomic_DNA. DR EMBL; AJ564539; CAD92206.1; -; Genomic_DNA. DR EMBL; AJ564540; CAD92207.1; -; Genomic_DNA. DR EMBL; AJ564541; CAD92208.1; -; Genomic_DNA. DR EMBL; AJ564542; CAD92209.1; -; Genomic_DNA. DR EMBL; AJ564543; CAD92210.1; -; Genomic_DNA. DR EMBL; AJ564544; CAD92211.1; -; Genomic_DNA. DR EMBL; AJ564545; CAD92212.1; -; Genomic_DNA. DR EMBL; AJ564546; CAD92213.1; -; Genomic_DNA. DR EMBL; AJ564547; CAD92214.1; -; Genomic_DNA. DR EMBL; AJ564548; CAD92215.1; -; Genomic_DNA. DR EMBL; AJ564549; CAD92216.1; -; Genomic_DNA. DR EMBL; AJ564550; CAD92217.1; -; Genomic_DNA. DR EMBL; AJ564551; CAD92218.1; -; Genomic_DNA. DR EMBL; AJ564552; CAD92219.1; -; Genomic_DNA. DR EMBL; AJ564553; CAD92220.1; -; Genomic_DNA. DR EMBL; AJ564554; CAD92221.1; -; Genomic_DNA. DR EMBL; AJ564555; CAD92222.1; -; Genomic_DNA. DR EMBL; AJ564556; CAD92223.1; -; Genomic_DNA. DR EMBL; AJ564557; CAD92224.1; -; Genomic_DNA. DR EMBL; AJ564558; CAD92225.1; -; Genomic_DNA. DR EMBL; AJ564559; CAD92226.1; -; Genomic_DNA. DR EMBL; AJ564560; CAD92227.1; -; Genomic_DNA. DR EMBL; AJ564561; CAD92228.1; -; Genomic_DNA. DR RefSeq; WP_000180650.1; NZ_JAHHIV020000001.1. DR RefSeq; WP_000180688.1; NZ_LSBF01000026.1. DR AlphaFoldDB; P0C601; -. DR SMR; P0C601; -. 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; 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..932 FT /note="2-oxoglutarate dehydrogenase E1 component" FT /id="PRO_0000224241" FT VARIANT 46..67 FT /note="Missing (in strain: SMH8997, LLA, LLE, SMH10501, FT SMH11888, SMH12248, SMH14017, SMH17487, SMH17608, SMH18000, FT SMH18034 and SMH18037)" FT VARIANT 534 FT /note="E -> D (in strain: 23, 3700, 3759, LIM1, LIM2 and FT LIM3)" FT VARIANT 864 FT /note="K -> N (in strain: 23, 3700, 3759, LIM1, LIM2 and FT LIM3)" SQ SEQUENCE 932 AA; 105383 MW; C744C1868AE20A38 CRC64; MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSIIKND DSIVPALKST SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV PKLEIEDFDL DQQTLEGISA GIVSDHFADI YDNAYEAILR MEKRYKGPIA FEYTHINNNT ERGWLKRRIE TPYKVTLNNN EKRALFKQLA YVEGFEKYLH KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM AHRGRLNVLT HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP IIIHGDAAYP GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA RSTTYSTDVA KGYDVPIFHV NADDVEATIE AIDIAMEFRK EFHKDVVIDL VGYRRFGHNE MDEPSITNPV PYQNIRKHDS VEYVFGKKLV NEGVISEDEM HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ ADEQSFTFDH LKEINDALLT YPDGFNILKK LNKVLEKRHE PFNKEDGLVD WAQAEQLAFA TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPDQKATF DIHNSPLSEA AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF SSRSKWGERS GLTLFLPHAY EGQGPEHSSA RLERFLQLAA ENNCTVVNLS SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK SLLRNKTVAK PIDEFTSGGF EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL LVAIERLYPF PEEEIEALLA QLPKLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN //