ID   ODO1_BRUO2              Reviewed;        1004 AA.
AC   A5VSQ0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; Synonyms=odhA; OrderedLocusNames=BOV_1852;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Paulsen I.;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000708; ABQ60359.1; -; Genomic_DNA.
DR   RefSeq; YP_001259747.1; -.
DR   GeneID; 5201823; -.
DR   GenomeReviews; CP000708_GR; BOV_1852.
DR   KEGG; bov:BOV_1852; -.
DR   TIGR; BOV_1852; -.
DR   OMA; A5VSQ0; 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   1004       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_1000065700.
SQ   SEQUENCE   1004 AA;  112573 MW;  4A5C3483F838816C CRC64;
     MAKQEQAPGR ANDVFALTSF LYGGNADYIE ELYAKYEDDP NSVDPQWRDF FAKLGDNADD
     VKKNAEGPSW TRKNWPIAAN GELVSALDGN WAEVEKHVTD KLKGKAAKGE AKGAAGTPLT
     AEEITQAARD SVRAIMMIRA YRMRGHLHAN LDPLGLAEKP NDYNELEPEN YGFTPADYNR
     KIFIDNVLGL EYATVPEMLD ILKRTYCGAI GVEFMHISDP AEKAWIQERI EGPDKKVAFT
     PEGKMAILSK LIEAEGFEQF IDVKYKGTKR FGLDGGESLI PALEQIVKRG GQMGLKEVVL
     GMAHRGRLNV LSQVMGKPHR AIFHEFKGGS YTPDDVEGSG DVKYHLGASS DREFDGNKVH
     LSLTANPSHL EIVNPVVMGK ARAKQDLLVG RTRDDMVPLS ERAKVLPLLL HGDAAFAGQG
     VVAECLGLSG LKGHRVAGTL HFIINNQIGF TTNPAFSRSS PYPSDVAKMI EAPIFHVNGD
     DPEAVVFAAK VATEFRMTFH KPVVIDMFCY RRFGHNEGDE PSFTQPLMYK AIRAHKTTVQ
     LYGEKLIAEG LVTQDDIDRM KADWRQKLEG EFEAGQSYKP NKADWLDGAW AGLRTADNAD
     EQRCGKTAVP VKTLKEIGKK LVEVPKDFHV HRTIQRFLDN RAKMMETGEG IDWATAESLA
     FGSLAVEGHP IRLSGQDVER GTFSQRHTVL YDQENQNRYI PLNNLQKGQA IYEAINSMLS
     EEAVLGYEYG YSLSDPRALV LWEAQFGDFA NGAQVVFDQF ISSGERKWLR MSGLVCLLPH
     GFEGQGPEHS SARLERYLQL CAEDNMQVAN VTTPANYFHI LRRQMKRDFR KPLIMMTPKS
     LLRHKRAIST LAELSGESSF HRLLWDDAQY NKDEGIKLQK DAKIRRVVLC SGKVYYDLYE
     EREKRGIDDV YLLRVEQLYP FPAKALINEL SRFRHAEMVW CQEEPKNMGA WSFIDPYLEW
     VLAHIDAKHQ RVRYAGRPAA ASPATGLMSK HLAQLAAFLE DALG
//