ID   ODO1_RICFE              Reviewed;         977 AA.
AC   Q4UKI8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 85.
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=RF_1092;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY61943.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000053; AAY61943.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041405326.1; NC_007109.1.
DR   AlphaFoldDB; Q4UKI8; -.
DR   SMR; Q4UKI8; -.
DR   STRING; 315456.RF_1092; -.
DR   EnsemblBacteria; AAY61943; AAY61943; RF_1092.
DR   KEGG; rfe:RF_1092; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 29166at2; -.
DR   Proteomes; UP000008548; 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; IPR005728; Rickett_RPE.
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.
DR   TIGRFAMs; TIGR01045; RPE1; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN           1..977
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000288750"
FT   DOMAIN          77..125
FT                   /note="RPE1 insert"
SQ   SEQUENCE   977 AA;  109496 MW;  B0B3FAD38BA0533F CRC64;
     MEEDLKKTGY LFGGNAVFVD ELYRQYLANP ASVDQTWQEF FAGIKDNSTV LNKSTAKIII
     PYEIKKEPLN NNLSSEVLNN RHLAKPAYRE EFKGDTERST AAYIDIREDA STGSTSKLPL
     EAKFGKMSSL KAKEMINTYR KHAHYLANLD PLGLELRKTK NDLKLNIETF GLDNSQLEKN
     INITDEFVGN WNCKLSELVT KLDKTYTGSI GVEFEQIENV EEKNWLYNKL ESEVTFSSED
     KKTILNDLVE VEGFEQYLHT KFPGAKRFSV EGGDASIVAM SKAIDLSMNQ GVEEIVIGMA
     HRGRLNTLTK VVGKPYKAVI AGFISGSVFP DELNVSGDVK YHLGYSSDRT IDNKKIHLSL
     ADNPSHLEAV NPIVAGKVRA KQDILGDTKR SKVKAILVHG DAAFCGQGVV AESLSMSPLA
     AYDIGGILHF VINNQLGFTA NAADTRASRY STEFAKIIAA PILHVNGDDI EAVLKATNIA
     VEYRQKFGKD VVVEIICYRK YGHNEGDEPM YTQGKMYNII KSKPTPGNIY ANELVKSGII
     DNNYFAKLKE EFKAKLDKEF EQAKNYKPEA HFLGGLWQGI SRIRTQAAIT GVGKKTLQDL
     GTKLCEIPKD FAVNPKLVKL FEARKATLTS DQPIDWATAE QLAFASLLSE GTNIRLTGQD
     CGRGTFSHRH SVLHNQIDDT TYIPLNNLSK TQAKYEVADS NLSEYAVLGF EYGYSLANPK
     NLVLWEAQFG DFANGAQIIF DQFISSSETK WLRMSGLVVL LPHAFEGQGP EHSSARLERF
     LQLAAEDNMY VTYPTTPASI FHLLRRQILD DTRKPLIIMS PKSLLRHKYA VSKLDELGEN
     TTFLPVLDEV NKVDTNNITK VILCSGKVYY DLFEMRGNNS NIAIIRLEQL YPFEKKLVAS
     LLKKYNRTQE FIWCQEEPKN MGAWRYIVSH LNDVLKEAGI NNEFKYVGRE ESASPAVGSL
     QAHNKQQEKL LKEALGM