ID   ODO1_BRUSU              Reviewed;        1004 AA.
AC   Q8FYF7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 37.
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=BR1923;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(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; AE014291; AAN30815.1; -; Genomic_DNA.
DR   RefSeq; NP_698900.1; -.
DR   GeneID; 1167623; -.
DR   GenomeReviews; AE014291_GR; BR1923.
DR   KEGG; bms:BR1923; -.
DR   NMPDR; fig|204722.1.peg.1857; -.
DR   TIGR; BR1923; -.
DR   HOGENOM; Q8FYF7; -.
DR   OMA; Q8FYF7; EGDEPAF.
DR   BioCyc; BSUI204722:BR_1923-MON; -.
DR   BRENDA; 1.2.4.2; 281610.
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_0000162171.
SQ   SEQUENCE   1004 AA;  112681 MW;  390B507D3018DD46 CRC64;
     MAKQEQAPDR ANDVFALTSF LYGGNADYIE ELYAKYEDDP NSVDPQWRDF FAKLGDNADD
     VKKNAEGPSW TRKNWPIAAN GELVSALDGN WAEVEKHVTD KLKGKAAKGE AKGAAGTPLT
     AEEITQAARD SVRAIMMIRA YRMRGHLHAN LDPLGLAEKP NDYNELEPEN YGFTPADYNR
     KIFIDNVLGL EYATVPEMLD ILKRTYCGAI GVEFMHISDP AEKAWIQERI EGPDKKVAFT
     PEGKKAILSK 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
     EQRRGKTAVP 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
//