ODO1_RICBR
ID ODO1_RICBR Reviewed; 927 AA.
AC Q1RHI4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN Name=sucA; OrderedLocusNames=RBE_1099;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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:0000250|UniProtKB:P0AFG3}.
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;
CC Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P0AFG3};
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:0000250|UniProtKB:P0AFG3}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000087; ABE05180.1; -; Genomic_DNA.
DR RefSeq; WP_011477758.1; NC_007940.1.
DR AlphaFoldDB; Q1RHI4; -.
DR SMR; Q1RHI4; -.
DR STRING; 336407.RBE_1099; -.
DR EnsemblBacteria; ABE05180; ABE05180; RBE_1099.
DR KEGG; rbe:RBE_1099; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 29166at2; -.
DR Proteomes; UP000001951; Chromosome.
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 Gene3D; 3.40.50.11610; -; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
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..927
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_0000288749"
SQ SEQUENCE 927 AA; 103677 MW; AAD6B2E0CEF8304E CRC64;
MEENLKKTGF LFGGNAVFIE ELYKQYLENP ASVDQTWQEF FSSVKDSNQL LNKSTAKIIL
KAAATEESKT SENPVSTTNN FNVGAMIKNY RKYAHYLAKL DPLGLEVTKT KEDLKLSIEN
FGFTNDQLSK VIEHKFLEKT YNLGELVNFL DKTYAGSIGV EFEQVENEEE KNWLYSKLES
GVISFSSEEK KNILNDLVEV EGFEQYLHTK FPGAKRFSVE GGDASIVAMN KAIDLSLHQG
VEEIVIGMAH RGRLNTLTKV VGKPYRAVIA GFISGSVFPD ELNVSGDVKY HLGYSSDRVV
GDKKIHLSLA DNPSHLEAVN PIFAGKVRAK QDMLKDNKRS KVKAILVHGD AAFCGQGVVA
ESLSMSPLAA YNIGGVLHFV INNQLGFTAN AADTRASRYS TEFAKIIAVP ILHVNGDDIE
AVLKATNIAV EYRQKFGKDV IVEIICYRKY GHNEGDEPMY TQGKMYNIIK SKLTPGNIYA
NELVKSGVID NNYFAKLKEQ FKAKLDKEYE QAKNYKQEAH FLGGLWQGIT RTRTQVAVTG
VDKKTLQSLG TKLCEMPKDF AVNPKLVKLF DARKAALTAD QPIDWATAEQ LAFASLLTSG
TNIRLTGQDC GRGTFSHRHS VLHNQVDDTT YIPLNNLSKE QATYEVADSN LSEYAVLGFE
YGYSLANPKN LVLWEAQFGD FANGAQIIFD QFISSSETKW LRMSGLVVLL PHGFEGQGPE
HSSARLERFL QLAAEDNMYV TYPTTPASIF HLLRRQIIDN VRKPLIVMSP KSLLRHKNVV
SKLDELGSNT TFLPVLDEVN KLEASNITKV ILCSGKVYYD LFEMRGSNSS IAIIRLEQLY
PFEKKVVVEL LKKYNKASEF IWCQEEPMNM GAWRYITSHL NNALKEAGIN NEFKYIGREE
SASPAVGSLQ AHNKQQEKLL KEALGVK