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   16-JUN-2009, entry version 27.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; OrderedLocusNames=RF_1092;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
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: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-
CC       oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC       succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
CC   -!- SIMILARITY: Contains 1 RPE1 insert domain.
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DR   EMBL; CP000053; AAY61943.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_247108.1; -.
DR   GeneID; 3400202; -.
DR   GenomeReviews; CP000053_GR; RF_1092.
DR   KEGG; rfe:RF_1092; -.
DR   NMPDR; fig|315456.3.peg.1091; -.
DR   HOGENOM; Q4UKI8; -.
DR   OMA; Q4UKI8; EGDEPAF.
DR   BioCyc; RFEL315456:RF_1092-MON; -.
DR   BRENDA; 1.2.4.2; 297363.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:EC.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR005728; Rickett_RPE.
DR   InterPro; IPR005475; Transketolase_central-reg.
DR   PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
DR   TIGRFAMs; TIGR01045; RPE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    977       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000288750.
FT   DOMAIN       77    125       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
//