ID   ODO1_STAAN              Reviewed;         910 AA.
AC   Q99U74;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=SA1245;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of
RT   S. aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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.
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DR   EMBL; BA000018; BAB42505.1; -; Genomic_DNA.
DR   PIR; E89918; E89918.
DR   RefSeq; NP_374526.1; -.
DR   GeneID; 1124084; -.
DR   GenomeReviews; BA000018_GR; SA1245.
DR   KEGG; sau:SA1245; -.
DR   HOGENOM; Q99U74; -.
DR   OMA; Q99U74; EGDEPAF.
DR   BioCyc; SAUR158879:SA1245-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   1: Evidence at protein level;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    910       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162178.
SQ   SEQUENCE   910 AA;  103112 MW;  7803AAED537CF247 CRC64;
     MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKRV MRLIDNIRQY
     GHLKADIYPV NPPKRKHVPK LEIEDFDLDQ QTLEGISAGI VSDHFADIYD NAYEAILRME
     KRYKGPIAFE YTHINNNTER GWLKRRIETP YKVTLNNNEK RALFKQLAYV EGFEKYLHKN
     FVGAKRFSIE GVDALVPMLQ RTITIAAKEG IKNIQIGMAH RGRLNVLTHV LEKPYEMMIS
     EFMHTDPMKF LPEDGSLQLT AGWTGDVKYH LGGIKTTDSY GTMQRIALAN NPSHLEIVAP
     VVEGRTRAAQ DDTQRAGAPT TDHHKAMPII IHGDAAYPGQ GINFETMNLG NLKGYSTGGS
     LHIITNNRIG FTTEPIDARS TTYSTDVAKG YDVPIFHVNA DDVEATIEAI DIAMEFRKEF
     HKDVVIDLVG YRRFGHNEMD EPSITNPVPY QNIRKHDSVE YVFGKKLVNE GVISEDEMHS
     FIEQVQKELR QAHDKINKAD KMDNPDMEKP AELALPLQAD EQSFTFDHLK EINDALLTYP
     DGFNILKKLN KVLEKRHEPF NKEDGLVDWA QAEQLAFATI LQDGTPIRLT GQDSERGTFS
     HRHAVLHDEQ TGETYTPLHH VPDQKATFDI HNSPLSEAAV VGFEYGYNVE NKKSFNIWEA
     QYGDFANMSQ MIFDNFLFSS RSKWGERSGL TLFLPHAYEG QGPEHSSARL ERFLQLAAEN
     NCTVVNLSSS SNYFHLLRAQ AASLDSEQMR PLVVMSPKSL LRNKTVAKPI DEFTSGGFEP
     ILTESYQADK VTKVILATGK MFIDLKEALA KNPDESVLLV AIERLYPFPE EEIEALLAQL
     PKLEEVSWVQ EEPKNQGAWL YVYPYVKVLV ADKYDLSYHG RIQRAAPAEG DGEIHKLVQN
     KIIENALKNN
//