ID ODO1_STAAW Reviewed; 932 AA. AC Q8NWR6; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=odhA; OrderedLocusNames=MW1303; OS Staphylococcus aureus (strain MW2). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., RA Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community- RT acquired MRSA."; RL Lancet 359:1819-1827(2002). 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; BA000033; BAB95168.1; -; Genomic_DNA. DR RefSeq; NP_646120.1; -. DR GeneID; 1003415; -. DR GenomeReviews; BA000033_GR; MW1303. DR KEGG; sam:MW1303; -. DR HOGENOM; Q8NWR6; -. DR OMA; Q8NWR6; EGDEPAF. DR BioCyc; SAUR196620:MW1303-MON; -. 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_0000162181. SQ SEQUENCE 932 AA; 105355 MW; CC7BA0F6E79E71AA 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 KPADLALPLQ 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 //