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 16-JUN-2009, entry version 9. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=odhA; OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacillales; 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 RT reduced susceptibility to vancomycin (VRSA) and hetero-VRSA (hVRSA)."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: 2- CC oxoglutarate dehydrogenase (E1), dihydrolipoamide CC succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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 BRENDA; 1.2.4.2; 95. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:HAMAP. DR GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01169; -; 1. DR InterPro; IPR011603; 2oxoglutarate_DH_E1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR005475; Transketolase_central-reg. DR PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1. DR Pfam; PF00676; E1_dh; 1. DR Pfam; PF02779; Transket_pyr; 1. DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1. DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1. PE 3: Inferred from homology; KW Glycolysis; Oxidoreductase; Thiamine pyrophosphate. FT CHAIN 1 932 2-oxoglutarate dehydrogenase E1 FT component. FT /FTId=PRO_0000224241. FT VARIANT 46 67 Missing (in strain: SMH8997, LLA, LLE, FT SMH10501, SMH11888, SMH12248, SMH14017, FT SMH17487, SMH17608, SMH18000, SMH18034 FT and SMH18037). FT VARIANT 534 534 E -> D (in strain: 23, 3700, 3759, LIM1, FT LIM2 and LIM3). FT VARIANT 864 864 K -> N (in strain: 23, 3700, 3759, LIM1, FT LIM2 and 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 //