ID   ODO1_STAHJ              Reviewed;         934 AA.
AC   Q4L6C4;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=SH1492;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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.
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; AP006716; BAE04801.1; -; Genomic_DNA.
DR   RefSeq; YP_253407.1; -.
DR   GeneID; 3481998; -.
DR   GenomeReviews; AP006716_GR; SH1492.
DR   KEGG; sha:SH1492; -.
DR   NMPDR; fig|279808.3.peg.2139; -.
DR   HOGENOM; Q4L6C4; -.
DR   OMA; Q4L6C4; FEEFLQI.
DR   BioCyc; SHAE279808:SH1492-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    934       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162184.
SQ   SEQUENCE   934 AA;  105479 MW;  7D9E801A49E880E9 CRC64;
     MAKDNKDVTE APVNFGANLG LMLDLYDDYL QDPSSVPDDL QVLFSTIKNG EAHVAAKSTT
     EGSGSSAGDG TIKRIMRLID NIRQYGHLKA DIYPVNAPKR TNLPKLEIEE FNLDKETLEN
     VSAEIVSDHF KDIYDNAYEA IERMEKRYKG PIAFEYNHIN NNKERTWLKR RIETPYRANI
     NNDERKKLFD TLAHVEGFEK YLHKNFVGAK RFSIEGVDTL VPMLQHTLKR AAEIEINNIQ
     IGMAHRGRLN VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTAGWTG DVKYHLGGVK
     TTSSYGIEQR ISLANNPSHL EIVAPVVIGK TRASQDDTKH AGKPTTDFHK GMPIIIHGDA
     AYPGQGINFE TMNLSNLDGY STGGALHIIT NNRIGFTTEP VDGRSTTYST DIAKGYDVPI
     LHVNADDVEA TIEAIDIAME FRKEFHKDFV IDLVGYRRYG HNEMDEPSIT NPLPYHNIRK
     HDSVEIIYGN KLVEDGVISK EQMEDVMDKV QKEMRAAQDK IDKSDKMDNP DMERPESLQE
     PLQSDDKDFS VDHLKEINDA MLTYPEDFHV LKKLNKVLEK RREPFESENG LVDWAQAEQL
     AFATIVQDGI SVRLTGQDSE RGTFSHRHAV LHDEENGDTF TPLHHVPNQK ATFEVHNSPL
     SEAAVVGFEY GYNVENKNSM NIWEAQYGDF SNMAQMMFDN FMSSARAKWG ERSGLTLFLP
     HAFEGQGPEH SSARLERFLQ LAAENNSTVV NLSSSSNYFH LLRAQAKSLG TEAMRPLIVM
     SPKSLLRNKT VAKPIDQFTS GGFKPIIVED GNKEKVTKLV LASGKMFIDL KEHLAKNPDD
     SILLVAVDRL YPFPEGEIKE VLNELPNLET VSWVQEEPKN QGAWLFVYPY LKSLVGNQFN
     LSYHGRIQRA APAEGDGEIH KLVQNQIIES SIEK
//