ID ODO1_OCEIH Reviewed; 953 AA. AC Q8CUL8; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 38. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=odhA; OrderedLocusNames=OB1089; OS Oceanobacillus iheyensis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=182710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831; RX MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya RT Ridge and its unexpected adaptive capabilities to extreme RT environments."; RL Nucleic Acids Res. 30:3927-3935(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. 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; BA000028; BAC13045.1; -; Genomic_DNA. DR RefSeq; NP_692010.1; -. DR GeneID; 1017056; -. DR GenomeReviews; BA000028_GR; OB1089. DR KEGG; oih:OB1089; -. DR NMPDR; fig|221109.1.peg.1090; -. DR HOGENOM; Q8CUL8; -. DR OMA; Q8CUL8; EGDEPAF. DR BioCyc; OIHE221109:OB1089-MON; -. DR BRENDA; 1.2.4.2; 278212. 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 1 953 2-oxoglutarate dehydrogenase E1 FT component. FT /FTId=PRO_0000162175. SQ SEQUENCE 953 AA; 107266 MW; 78AB32B7CFBE7A6E CRC64; MAENAESAER FWGQFHGQNT GYLEQQFELY KEDPELVESS IRTIFDTHGA PSWLSSTENV KSVSNASDFD VTKLTSAIRL VEAIRRYGHT DADIYPVGGY KGDRSKMLDL STYNLKEQDL EKIPASWIWE KQAPGVATAL DVVNQLKKYY TGTITFEYDH VNNDEERKWL FDLIEEGNAR LDPSDDERKK ILQRLADVEG FEKFLHKTFV GQKRFSIEGL ESMVPMIDHI VQYSNQDSIE HVMMGMAHRG RLSVLANVLG KPYDKIFSEF NYTKEKELMP SEGSRAINYG WTGDVKYHYG AEKEVEFGNK GQTRITLAHN PSHLEFVNPV VEGFTRAAQD DRSEKGYPKQ VTNKAVSVLI HGDAAFIGEG VVAETLNLSG LPGYSTGGTL HIIANNLLGY TTDREDGRST RYASDLAKGF EIPVIRVNAD DPISCISAIK IAYEYRQKFQ KDFLIDLVGY RRYGHNEMDE PRTTQPSLYQ QIDDHPSVAS LFGKGMEEKG ILQEGGFEEV KSAVEKKLTD IYKGMTESEI GEPEAKLMPQ VLTNGLDQFT TAIDLATLKS INEELLERPE GFKGFKKTER ILQRRKDALE EGNKADWGTG EALAFASILK EGTPIRLTGQ DTERGTFAHR HIVLHDVETG EKYSPLHGLS DVEASFDVRN SPLSEAGVLG FEYGYSVQSP DTLVIWEAQF GDFANAGQVI FDQFISSARA KWGEKSNMVL LLPHGYEGQG PEHSSARLER FLQMAAENNW IVANVTSSAQ LFHILRRQAA MRDRDEARPL VLMTPKSSLI RHPRMGATAE EFTDGGFLAL RDQPGFEANR EKVTRLVVGS GKMMIDIEEA MDDSDETYDW LQIKRVEQIY PFPKKALEEE IKQLPNLKEI VWVQEEPKNM GAWNFVDDYL RELLNEDQKL KVISRPDRSA PAGGIPTVHK TAQNKIIKQA LNQSEGGKSS AGN //