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   27-MAR-2024, entry version 95.
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; Pseudomonadota; 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=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, 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   KEGG; rbe:RBE_1099; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
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   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 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   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Reference proteome; 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
//