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   25-MAY-2022, entry version 77.
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; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; 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., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., 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: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC         COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000255|HAMAP-
CC       Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR   EMBL; CP000872; ABX62957.1; -; Genomic_DNA.
DR   RefSeq; WP_004692111.1; NC_010103.1.
DR   AlphaFoldDB; A9M8Q9; -.
DR   SMR; A9M8Q9; -.
DR   EnsemblBacteria; ABX62957; ABX62957; BCAN_A1967.
DR   GeneID; 55591514; -.
DR   KEGG; bcs:BCAN_A1967; -.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OMA; RDSYCRT; -.
DR   PhylomeDB; A9M8Q9; -.
DR   Proteomes; UP000001385; Chromosome I.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.50.11610; -; 1.
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; IPR042179; KGD_C_sf.
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   Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN           1..1004
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="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