ID   ODO1_STAS1              Reviewed;         933 AA.
AC   Q49XM5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=SSP1325;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18470.1; -; Genomic_DNA.
DR   RefSeq; YP_301415.1; -.
DR   GeneID; 3616663; -.
DR   GenomeReviews; AP008934_GR; SSP1325.
DR   KEGG; ssp:SSP1325; -.
DR   NMPDR; fig|342451.4.peg.605; -.
DR   HOGENOM; Q49XM5; -.
DR   OMA; Q49XM5; MELACEW.
DR   BioCyc; SSAP342451:SSP1325-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    933       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162185.
SQ   SEQUENCE   933 AA;  105479 MW;  603C12A85D1562EB CRC64;
     MSNESQVSEA PVNFGANLGY VLDLYDIYLD NPSAVPEDLQ VLFSTIKNGE ANIATNTEGQ
     SNVTKGDSTI KRVMRLIDNI RQYGHLLADI YPVNRPQREN VPKLNMEDFN LDQETLESIS
     AGIVSEHFKD IYDNAYEAIV RMEKRYKGPI AFEYTHINNN RERVWLKRRI ETPYKATLND
     NQKIELFKNL AHVEGFEKYL HKNFVGAKRF SIEGVDTLVP MLQQTLRIAS DEGIQNIQIG
     MAHRGRLNVL THVLEKPYEM MISEFMHIDP MKFLPEDGSL QLTSGWTGDV KYHLGGVKTT
     QSYGSEQRIS LANNPSHLEI VAPVVLGKTR ANQDTTDKPG AVTTEFKKSM PILIHGDAAY
     PGQGINFEAM NLGNLEGYST GGSLHIITNN RIGFTTEPED GRSTTYSSDV AKGYDVPIMH
     VNADNVEATI EAIEIAMAFR KEFNKDVVID LVGYRRYGHN EMDEPSITNP LQYYEIRKHE
     SVDILYGKQL VNENIISENQ MNQIFDDVQN TLRAAHDKID KNDKMDNPDM QKPDSLAEPI
     QTKDEEVSYE QLKEINDAML SYPSDFNVLK KLNKVLEKRR EPFESEDGLV DWAQAEQLAF
     ATITQNGRPI RLTGQDSERG TFSHRHAVLH DPDTGAQYVP LHNVPDQKAT FEVRNSPLSE
     AAVVGFEYGY NIQNKSCMTI WEAQYGDFSN MAQMIFDNFL FSSRAKWGER SGLTLFLPHS
     FEGQGPEHSS ARLERFLQLA GENNSTIVNL SSSSNYFHLL RAQAANLGTQ SMRPLVVMSP
     KSLLRNKTVA DPISKFTSGK FEPILPEAHD KASVKKVILA SGKMFIDLKE YLTKNPNKSI
     LLVAVERLYP FPADEIDALL SELPNLEHVA WVQEEPKNQG AWSFVYPYLK ELTTDKYDLS
     YHGRIQRSAP AEGDGEIHKL VQNMIIEQST NIN
//