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Database: UniProt/SWISS-PROT
Entry: ODO1_BRUC2
LinkDB: ODO1_BRUC2
Original site: ODO1_BRUC2 
ID   ODO1_BRUC2              Reviewed;        1004 AA.
AC   A9M8Q9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   23-MAY-2018, entry version 63.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=sucA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Synonyms=odhA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=BCAN_A1967;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-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).
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01169}.
DR   EMBL; CP000872; ABX62957.1; -; Genomic_DNA.
DR   RefSeq; WP_004692111.1; NC_010103.1.
DR   ProteinModelPortal; A9M8Q9; -.
DR   SMR; A9M8Q9; -.
DR   PRIDE; A9M8Q9; -.
DR   EnsemblBacteria; ABX62957; ABX62957; BCAN_A1967.
DR   KEGG; bcs:BCAN_A1967; -.
DR   HOGENOM; HOG000259586; -.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   BioCyc; BCAN483179:G1GAF-1907-MONOMER; -.
DR   Proteomes; UP000001385; Chromosome I.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
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_1000085385.
SQ   SEQUENCE   1004 AA;  112651 MW;  C7F7EC096BEB3301 CRC64;
     MAKQEQAPDR ANDVFALTSF LYGGNADYIE ELYAKYEDDP NSVDPQWRDF FAKLGDNADD
     VKKNAEGPSW TRKNWPIAAN GELVSALDGN WAEVEKHVAD 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
//
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