ODO1_BRUSU
ID ODO1_BRUSU Reviewed; 1004 AA.
AC Q8FYF7; G0K866;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=BR1923, BS1330_I1917;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX 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., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30815.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19232.1; -; Genomic_DNA.
DR RefSeq; WP_004687685.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FYF7; -.
DR SMR; Q8FYF7; -.
DR EnsemblBacteria; AEM19232; AEM19232; BS1330_I1917.
DR GeneID; 45052873; -.
DR KEGG; bms:BR1923; -.
DR KEGG; bsi:BS1330_I1917; -.
DR PATRIC; fig|204722.21.peg.2974; -.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OMA; RDSYCRT; -.
DR PhylomeDB; Q8FYF7; -.
DR Proteomes; UP000007104; 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_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
