ID   ODO1_ECOL6              Reviewed;         933 AA.
AC   P0AFG4; P07015; P78225;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-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=sucA; OrderedLocusNames=c0803;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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.
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DR   EMBL; AE014075; AAN79276.1; -; Genomic_DNA.
DR   RefSeq; NP_752733.1; -.
DR   GeneID; 1035834; -.
DR   GenomeReviews; AE014075_GR; c0803.
DR   KEGG; ecc:c0803; -.
DR   HOGENOM; P0AFG4; -.
DR   OMA; P0AFG4; EGDEPAF.
DR   BRENDA; 1.2.4.2; 292881.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:EC.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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_0000162193.
SQ   SEQUENCE   933 AA;  105062 MW;  EAEF8429EC31E749 CRC64;
     MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQFHS
     QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWQQDKV
     ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLEAL KQTYCGPIGA EYMHITSTEE
     KRWIQQRIES GRATFNSEEK KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK
     EMIRHAGNSG TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG
     FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL PITIHGDAAV
     TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF
     HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH
     PTPRKIYADK LEQEKVATLE DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE
     WDEEYPNKVE MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA
     YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG AFRVWDSVLS
     EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH
     GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS
     LLRHPLAVSS LEELANGTFL PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV
     AIVRIEQLYP FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR
     YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE
//