ID   ODO1_RICCN              Reviewed;         928 AA.
AC   Q92J42;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=RC0227;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02765.1; -; Genomic_DNA.
DR   PIR; C97728; C97728.
DR   RefSeq; WP_010976891.1; NC_003103.1.
DR   AlphaFoldDB; Q92J42; -.
DR   SMR; Q92J42; -.
DR   EnsemblBacteria; AAL02765; AAL02765; RC0227.
DR   KEGG; rco:RC0227; -.
DR   PATRIC; fig|272944.4.peg.262; -.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OMA; RDSYCRT; -.
DR   Proteomes; UP000000816; 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..928
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162195"
SQ   SEQUENCE   928 AA;  103801 MW;  4468B7CE1901591D CRC64;
     MGEDFKKTGY LFGGNAVFVE ELYKQYLANP ASVDQTWQEF FAGIKDNNTL LNKSTAKIII
     PDEIKKESLN NNLSSEDLNS LKAKEMINAY RKHAHYLANL DPLGLELRKT KNDLKLNIET
     FGLDSGQLEE NINITDEFVG TWNCKLSELV TKFDKVYTGS IGVEFEQIEN VAGKNWLYNK
     LESEVTFSSE DKKTILNDLV EVEGFEQYLH TKFPGAKRFS IEGGDASIVA MSKAIDLSMH
     QGVSEIVIGM AHRGRLNTLT KVVGKPYKAV IADFISGSVF PDELNVSGDV KYHLGYSSDR
     TLEDKKIHLS LADNPSHLEA VNPIVAGKVR AKQDILGDTK RSKVKAILVH GDAAFCGQGV
     VAESLSMSPL AAYDIGGILH FVINNQLGFT ANAADTRASR YSTEFAKIIA APILHVNGDD
     IEAVLKATNI AVEYRQKFGK DVVVEIICYR KYGHNEGDEP MYTQGKMYNI IKNKLTPGNI
     YANELVKSGV IDNNYFAKLK EEFKAKLDKE YEQAKSYKQE AHFLGGLWQG ISRTRTQATI
     TGISKKTLHD LGTKLCEIPK DFAVNPKLVK LFEARKATLT ADQPIDWATA EQLAFASLLA
     SGTNIRLTGQ DSGRGTFSHR HSVLHNQIDG TTYIPLNNLS KEQAKYEVAD SNLSEYAVLG
     FEYGYSLANP KNLVLWEAQF GDFANGAQII FDQFISSSET KWLRMSGLVV LLPHAFEGQG
     PEHSSARLER FLQLAAENNM YVTYPTTPAS IFHLLRRQIL DDTRKPLIVM SPKSLLRHKY
     AVSKLDELGE NTTFLPVLDE VTKVDTNNIT KVILCSGKVY YDLFEMRGNN SNIAIIRLEQ
     LYPFEKKLVA SLLKKYNRTQ EFIWCQEEPK NMGTWCYIVS HLNDALKEAG IKNEFKYVGR
     EESASPAVGS LQVHNKQQEK LLRTALGI