ID ODO1_STAA9 Reviewed; 932 AA. AC A5ISU5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=odhA; OrderedLocusNames=SaurJH9_1474; OS Staphylococcus aureus (strain JH9). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=359786; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.; RT "Complete sequence of chromosome of Staphylococcus aureus subsp. RT aureus JH9."; RL Submitted (MAY-2007) 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; CP000703; ABQ49268.1; -; Genomic_DNA. DR RefSeq; YP_001246844.1; -. DR GeneID; 5168710; -. DR GenomeReviews; CP000703_GR; SaurJH9_1474. DR KEGG; saj:SaurJH9_1474; -. DR OMA; A5ISU5; EGDEPAF. 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 Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate. FT CHAIN 1 932 2-oxoglutarate dehydrogenase E1 FT component. FT /FTId=PRO_1000085388. SQ SEQUENCE 932 AA; 105357 MW; F671CE1A65ADAF6D CRC64; MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND 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 QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN //