ID   ODO1_CORGL              Reviewed;        1257 AA.
AC   Q8NRC3; P96746; Q6M641;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=Cgl1129, cg1280;
OS   Corynebacterium glutamicum (Brevibacterium flavum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=AJ12036;
RX   MEDLINE=97158227; PubMed=9004499;
RA   Usuda Y., Tujimoto N., Abe C., Asakura Y., Kimura E., Kawahara Y.,
RA   Kurahashi O., Matsui H.;
RT   "Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium
RT   lactofermentum' AJ12036) odhA gene encoding a novel type of 2-
RT   oxoglutarate dehydrogenase.";
RL   Microbiology 142:3347-3354(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RA   Nakagawa S.;
RT   "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INHIBITION BY ODHI.
RX   PubMed=16522631; DOI=10.1074/jbc.M512515200;
RA   Niebisch A., Kabus A., Schultz C., Weil B., Bott M.;
RT   "Corynebacterial protein kinase G controls 2-oxoglutarate
RT   dehydrogenase activity via the phosphorylation status of the OdhI
RT   protein.";
RL   J. Biol. Chem. 281:12300-12307(2006).
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   -!- ENZYME REGULATION: Inhibited by unphosphorylated odhI, but not by
CC       phosphorylated odhI.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
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DR   EMBL; D84102; BAA12222.2; ALT_INIT; Genomic_DNA.
DR   EMBL; BX927151; CAF19835.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98522.1; -; Genomic_DNA.
DR   RefSeq; NP_600357.3; -.
DR   RefSeq; YP_225421.2; -.
DR   HSSP; P07016; 1E2O.
DR   GeneID; 1019114; -.
DR   GeneID; 3343144; -.
DR   GenomeReviews; BA000036_GR; Cgl1129.
DR   GenomeReviews; BX927147_GR; cg1280.
DR   KEGG; cgb:cg1280; -.
DR   KEGG; cgl:NCgl1084; -.
DR   HOGENOM; Q8NRC3; -.
DR   OMA; Q8NRC3; EGDEPAF.
DR   BioCyc; CGLU196627-1:CG1280-MON; -.
DR   BRENDA; 1.2.4.2; 812.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:InterPro.
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; IPR001078; 2-oxoacid_DH_actylTfrase.
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; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   ProDom; PD001115; 2Oxoacid_dh; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1   1257       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000273521.
FT   CONFLICT     20     20       T -> I (in Ref. 1; BAA12222).
FT   CONFLICT     80     80       T -> A (in Ref. 1; BAA12222).
FT   CONFLICT    118    118       D -> A (in Ref. 1; BAA12222).
FT   CONFLICT    274    274       A -> T (in Ref. 1; BAA12222).
FT   CONFLICT    449    449       N -> S (in Ref. 1; BAA12222).
FT   CONFLICT    460    460       N -> S (in Ref. 1; BAA12222).
FT   CONFLICT   1003   1003       I -> V (in Ref. 1; BAA12222).
FT   CONFLICT   1129   1129       N -> D (in Ref. 1; BAA12222).
SQ   SEQUENCE   1257 AA;  138757 MW;  96473BCB12B22ABF CRC64;
     MLQLGLRHNQ PTTNVTVDKT KLNKPSRSKE KRRVPAVSSA STFGQNAWLV DEMFQQFQKD
     PKSVDKEWRE LFEAQGGPNT TPATTEAQPS APKESAKPAP KAAPAAKAAP RVETKPADKT
     APKAKESSVP QQPKLPEPGQ TPIRGIFKSI AKNMDISLEI PTATSVRDMP ARLMFENRAM
     VNDQLKRTRG GKISFTHIIG YAMVKAVMAH PDMNNSYDVI DGKPTLIVPE HINLGLAIDL
     PQKDGSRALV VAAIKETEKM NFSEFLAAYE DIVARSRKGK LTMDDYQGVT VSLTNPGGIG
     TRHSVPRLTK GQGTIIGVGS MDYPAEFQGA SEDRLAELGV GKLVTITSTY DHRVIQGAVS
     GEFLRTMSRL LTDDSFWDEI FDAMNVPYTP MRWAQDVPNT GVDKNTRVMQ LIEAYRSRGH
     LIADTNPLSW VQPGMPVPDH RDLDIETHNL TIWDLDRTFN VGGFGGKETM TLREVLSRLR
     AAYTLKVGSE YTHILDRDER TWLQDRLEAG MPKPTQAEQK YILQKLNAAE AFENFLQTKY
     VGQKRFSLEG AEALIPLMDS AIDTAAGQGL DEVVIGMPHR GRLNVLFNIV GKPLASIFNE
     FEGQMEQGQI GGSGDVKYHL GSEGQHLQMF GDGEIKVSLT ANPSHLEAVN PVMEGIVRAK
     QDYLDKGVDG KTVVPLLLHG DAAFAGLGIV PETINLAKLR GYDVGGTIHI VVNNQIGFTT
     TPDSSRSMHY ATDYAKAFGC PVFHVNGDDP EAVVWVGQLA TEYRRRFGKD VFIDLVCYRL
     RGHNEADDPS MTQPKMYELI TGRETVRAQY TEDLLGRGDL SNEDAEAVVR DFHDQMESVF
     NEVKEGGKKQ AEAQTGITGS QKLPHGLETN ISREELLELG QAFANTPEGF NYHPRVAPVA
     KKRVSSVTEG GIDWAWGELL AFGSLANSGR LVRLAGEDSR RGTFTQRHAV AIDPATAEEF
     NPLHELAQSK GNNGKFLVYN SALTEYAGMG FEYGYSVGNE DSIVAWEAQF GDFANGAQTI
     IDEYVSSGEA KWGQTSKLIL LLPHGYEGQG PDHSSARIER FLQLCAEGSM TVAQPSTPAN
     HFHLLRRHAL SDLKRPLVIF TPKSMLRNKA AASAPEDFTE VTKFQSVIND PNVADAAKVK
     KVMLVSGKLY YELAKRKEKD GRDDIAIVRI EMLHPIPFNR ISEALAGYPN AEEVLFVQDE
     PANQGPWPFY QEHLPELIPN MPKMRRVSRR AQSSTATGVA KVHQLEEKQL IDEAFEA
//