ID   ODO1_RICPR              Reviewed;         936 AA.
AC   Q9ZDY3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=RP180;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14647.1; -; Genomic_DNA.
DR   PIR; H71728; H71728.
DR   RefSeq; NP_220570.1; NC_000963.1.
DR   RefSeq; WP_004598613.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDY3; -.
DR   SMR; Q9ZDY3; -.
DR   STRING; 272947.gene:17555263; -.
DR   EnsemblBacteria; CAA14647; CAA14647; CAA14647.
DR   GeneID; 57569308; -.
DR   KEGG; rpr:RP180; -.
DR   PATRIC; fig|272947.5.peg.185; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000002480; 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..936
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162196"
SQ   SEQUENCE   936 AA;  105796 MW;  30EA24895B4758AC CRC64;
     MEEYFNKTGY LFSGNAVFVE ELYRQYLANP NSVDQTWQEF FADIKDNNVV LNKSTAKVIS
     TNVTNKELLN NNLSSETLNN LKAKEMISAY RRNAHYLANL DPLGLEIRKT KNDLKLNIEA
     FGLDSSQLGE NINIMDEFIG TWNCKLSELV TKLDKVYTSS IGVEFDQIEN VEEKNWLYTK
     LETDITFTSE EKKSILNDLV EVECFEQFLH IKFPGAKRFS IEGGDASIVA MNKAIDLSMH
     QGVEEIVIGM AHRGRLNTLT KVVGKPYKEV IASFINGNIF PDGLNVSGDV KYHLGYSADR
     VRANQKIHLS LADNPSHLEA INSIVAGKVR AKQDIFVDTK RSKIKAILVH GDAAFCGQGV
     VAESLSMSPL TAYNVGGILH FVINNQLGFT ANAADTRASR YSTEFAKIIS APILHVNGDD
     IEAVLKATDI AVEYRQKFSK DVVVEIICYR KYGHNEGDEP MYTQSKMYNI IKSKPTPGSI
     YANELVKNGI IDNNYYAKLK EKFKIRLDQE YEQAKSYKQE THFFEGYWKG ISRIRGKDAI
     TGVNKKILQD LGTKLCEIPK DFAINPKLIR LFEVRKTTLT TDQPIDWATA EQLAFAHLLC
     SGINIRLTGQ DSARGTFSHR HSILHNQIDD TTYIPLNNLS KTQAKYEVAN SNLSEYAALG
     FEYGYSLANP KNLVLWEAQF GDFANGAQII FDQFISSSAT KWLRMSGLVV LLPHAFEGQG
     PEHSSARLER FLQLAAEENM YITYPTTPAS IFHLLRRQIL ESTRKPLIVM SPKSLLRHKY
     AVSKLDELGE NTTFIPILDE VTKIDTNNVT KVILCSGKVY YDLFAMRTNN SNIVIIRLEQ
     LYPFEKKLVA SLLKKYNKAQ AFIWCQEEPK NMGAWHYIAT HLNDALKEAE INNEFKYVGR
     EESASPAVGS LQVHNKQQEK LLMEALGDDI IKEKLY
//