ID   ODO1_RICTY              Reviewed;         933 AA.
AC   Q68XI7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=RT0171;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03655.1; -; Genomic_DNA.
DR   RefSeq; WP_011190642.1; NC_006142.1.
DR   AlphaFoldDB; Q68XI7; -.
DR   SMR; Q68XI7; -.
DR   STRING; 257363.RT0171; -.
DR   EnsemblBacteria; AAU03655; AAU03655; RT0171.
DR   KEGG; rty:RT0171; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   Proteomes; UP000000604; 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..933
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000288751"
SQ   SEQUENCE   933 AA;  105257 MW;  FD32A523811440FB CRC64;
     MEKYFNKTGY LFAGNAVFVE ELYRQYLANP NSVDQTWQEF FADIKDNNAL LNKSTAKVIR
     PNPNVTKALL NNNLSYEGLH NLKAKEMISA YRRNAHYLAN LDPLGLEIRK TKDELKLNIE
     AFGLDSSQLE ENINITDEFI GTWNCKLSEL VTKLDKVYTS SIGVEFDQIE NVEEKNWLYT
     KLETEITFAS EEKRSILNDF VEVECFEQFL HTKFPGAKRF SIEGGDSSIV AMNKAIDLSM
     NQGVEEIVIG MAHRGRLNTL TKVVGKPYKA VIAGFINGNV FPDELNISGD VKYHLGYSAD
     RVRANQKIHL SLADNPSHLE AINSIVAGKV RAKQDMLVDT KRSKVKAILL HGDAAFCGQG
     VVAESLSMSP LTAYNVGGIL HFVINNQLGF TANAADTRAS RYSTEFAKII AAPILHVNGD
     DIEAVLKATD IAVEYRQKFS KDVVVEIICY RKYGHNEGDE PMYTQSKMYN IIKSKPTPGN
     IYANELVKSG IIDNNYYAKL KEKFKIKLDK EYEQAKSYKQ ESHFLGGCWK GISRTRGKAA
     ITGVNKKILQ DLGTKLCEIP KDFTINPKLV RLFEVRKNTL TTDQPIDWAT AEQLAFAHLL
     CSGTNIRLTG QDSERGTFSH RHSILHNQID DTTYIPLNNL SKTQAQYEVA NSNLAEYAVL
     GFEYGYSLAS PKNLVLWEAQ FGDFANGAQI IFDQFISSSA TKWLRMSGLV VLLPHAFEGQ
     GPEHSSARLE RFLQLAAEEN MYITYPTTPA SIFHLLRRQI LESIRKPLIV MSPKSLLRHK
     YAVSKLDELG ENTTFIPVLD EVTKIDKNNI TKVILCSGKV YYDLFAKRVH NSNIVIIRLE
     QLYPFEKTLV ASLLKKYNKA QAFIWCQEEP KNMGAWNYIA EHLNDALKEA EINNEFKYVG
     REESASPAVG SLQVHNKQQE KLLMEALGDD IIK