ID ODO1_BACA2 Reviewed; 944 AA. AC A7Z5J9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 12. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=odhA; OrderedLocusNames=RBAM_019130; OS Bacillus amyloliquefaciens (strain FZB42). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). 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; CP000560; ABS74275.1; -; Genomic_DNA. DR RefSeq; YP_001421506.1; -. DR GeneID; 5461918; -. DR GenomeReviews; CP000560_GR; RBAM_019130. DR KEGG; bay:RBAM_019130; -. DR OMA; A7Z5J9; EGDEPAF. 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 1 944 2-oxoglutarate dehydrogenase E1 FT component. FT /FTId=PRO_1000065696. SQ SEQUENCE 944 AA; 106267 MW; 936E7315F09C54CD CRC64; MFQNNMKQRM NWEDFYGPNL GYALELYDQY AEDPDSIDPD LKDMFDELGA PPSQIKEASG TKEQGRVTAD LIQKIAAAVK LAEDIRTYGH LNASVNPLRK DPKKSELFPL SDYGLTEEEM KAIPASVICK DAPANITNGL EAIQHLRNTY KRTISFEFDH VHDFEERAWI TKMVESGELF RKNSPEKLSA VLERLTEVEG FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKAGTT NVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSTGISYG WTGDVKYHLG ADRQLQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQKGYPVQ DETKSLAILI HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF TTESDESRST KYASDLAKGY EIPIVHVNAD DPEACLSAVK FAVEYRKRFN KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD AVRKHPTVKR IFAEKLVSEG LISEEKAQNI ETAVTKRIED AYKKVPAKKE DAVREIELPE PVSNGFPDVD TAIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG EEFVALHHLD DCAASFTVHN SPLSEGSVLG FEYGYNVYSP ETLVMWEAQY GDFANAAQVY FDQFISAGRA KWGQKSGLVM LLPHGYEGQG PEHSSGRVER FLQLAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL VIMTPKSLLR NPNTVSEVQE LSESRFKPVY EQSGLSHAYE KVTRVVLSSG KVSIDISDHF NKMEGDKDWL HIARIEQLYP FPAKDTKELF AKLPNLQEIV WVQEEPQNMG AWSYISPYLS EIAPKGVNVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN //