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Database: UniProt/SWISS-PROT
Entry: ODO1_STAES
LinkDB: ODO1_STAES
Original site: ODO1_STAES 
ID   ODO1_STAES              Reviewed;         934 AA.
AC   Q8CP83;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   28-FEB-2018, entry version 91.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=odhA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=SE_1097;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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).
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01169}.
DR   EMBL; AE015929; AAO04694.1; -; Genomic_DNA.
DR   RefSeq; NP_764652.1; NC_004461.1.
DR   RefSeq; WP_002456517.1; NC_004461.1.
DR   ProteinModelPortal; Q8CP83; -.
DR   SMR; Q8CP83; -.
DR   STRING; 176280.SE1097; -.
DR   PRIDE; Q8CP83; -.
DR   EnsemblBacteria; AAO04694; AAO04694; SE_1097.
DR   GeneID; 1057037; -.
DR   KEGG; sep:SE1097; -.
DR   PATRIC; fig|176280.10.peg.1073; -.
DR   eggNOG; ENOG4105C7P; Bacteria.
DR   eggNOG; COG0567; LUCA.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   BioCyc; SEPI176280:G1G05-1103-MONOMER; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    934       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162183.
SQ   SEQUENCE   934 AA;  105693 MW;  DD892FD718D6C28A CRC64;
     MTKNKKEFTE APVNFGANLG LMLDLYDDYL QDPSSVPEDL QVLFSTIKTG EAHIEAKPTT
     DGGGSQAGDS TIKRVMRLID NIRQYGHLKA DIYPVNPPER QNVPKLEIED FDLDKETLEK
     ISSGIVSEHF KDIYDNAYDA IVRMERRYKG PIAFEYTHIN NNKERVWLKR RIETPYKASL
     NDNQKKELFK KLAHVEGFEK YLHKNFVGAK RFSIEGVDTL VPMLQHTITL AGNEGIKNIQ
     IGMAHRGRLN VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTSGWTS DVKYHLGGVK
     TTNSYGIEQR ISLANNPSHL EIVAPVVAGK TRAAQDNTHQ VGAPSTDFHK AMPIIIHGDA
     AYPGQGINFE TMNLGSLKGY STGGSLHIIT NNRIGFTTEP IDGRSTTYSS DVAKGYDVPI
     LHVNADDVEA TIEAIEIAME FRKEFHKDVV IDLVGYRRYG HNEMDEPSIT NPVPYQNIRK
     HDSVEILYGK KLVDEGIISE DEMNEVIDGV QKEMRTAHDK IDKNDKMNNP DMEKPESLQL
     PLQSDTKDFS FDHLKEINDA MLDYPKDFHV LKKLNKVLEK RREPFEKEEG LVDWAQAEQL
     AFATILQDGT SIRLTGQDSE RGTFSHRHAV LHDEENGNTF TPLHHVPQQQ ATFDIHNSPL
     SEAAVVGFEY GYNVENKGNF NIWEAQYGDF SNMSQMMFDN FLSSSRAKWG ERSGLTLFLP
     HAFEGQGPEH SSARLERFLQ LAAENNSTVV NLSSASNYFH LLRAQAASLD TLEMRPLIVM
     SPKSLLRNKT VAKPIDEFTS GGFKPIITED IDEQKVKKVI LASGKMYIDL KEYLAKNPND
     SILLIAVERL YPFPEEEIKE VLKSLPHLEN VSWVQEEPKN QGAWLFVYPY LKALVANKYD
     LTYHGRIQRA APAEGDGEIH KLVQTKIIES SINN
//
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