ID   ODO1_RICBR              Reviewed;         927 AA.
AC   Q1RHI4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; OrderedLocusNames=RBE_1099;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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.
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DR   EMBL; CP000087; ABE05180.1; -; Genomic_DNA.
DR   RefSeq; YP_538269.1; -.
DR   GeneID; 3995010; -.
DR   GenomeReviews; CP000087_GR; RBE_1099.
DR   KEGG; rbe:RBE_1099; -.
DR   HOGENOM; Q1RHI4; -.
DR   OMA; Q1RHI4; EGDEPAF.
DR   BioCyc; RBEL336407:RBE_1099-MON; -.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    927       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000288749.
SQ   SEQUENCE   927 AA;  103677 MW;  AAD6B2E0CEF8304E CRC64;
     MEENLKKTGF LFGGNAVFIE ELYKQYLENP ASVDQTWQEF FSSVKDSNQL LNKSTAKIIL
     KAAATEESKT SENPVSTTNN FNVGAMIKNY RKYAHYLAKL DPLGLEVTKT KEDLKLSIEN
     FGFTNDQLSK VIEHKFLEKT YNLGELVNFL DKTYAGSIGV EFEQVENEEE KNWLYSKLES
     GVISFSSEEK KNILNDLVEV EGFEQYLHTK FPGAKRFSVE GGDASIVAMN KAIDLSLHQG
     VEEIVIGMAH RGRLNTLTKV VGKPYRAVIA GFISGSVFPD ELNVSGDVKY HLGYSSDRVV
     GDKKIHLSLA DNPSHLEAVN PIFAGKVRAK QDMLKDNKRS KVKAILVHGD AAFCGQGVVA
     ESLSMSPLAA YNIGGVLHFV INNQLGFTAN AADTRASRYS TEFAKIIAVP ILHVNGDDIE
     AVLKATNIAV EYRQKFGKDV IVEIICYRKY GHNEGDEPMY TQGKMYNIIK SKLTPGNIYA
     NELVKSGVID NNYFAKLKEQ FKAKLDKEYE QAKNYKQEAH FLGGLWQGIT RTRTQVAVTG
     VDKKTLQSLG TKLCEMPKDF AVNPKLVKLF DARKAALTAD QPIDWATAEQ LAFASLLTSG
     TNIRLTGQDC GRGTFSHRHS VLHNQVDDTT YIPLNNLSKE QATYEVADSN LSEYAVLGFE
     YGYSLANPKN LVLWEAQFGD FANGAQIIFD QFISSSETKW LRMSGLVVLL PHGFEGQGPE
     HSSARLERFL QLAAEDNMYV TYPTTPASIF HLLRRQIIDN VRKPLIVMSP KSLLRHKNVV
     SKLDELGSNT TFLPVLDEVN KLEASNITKV ILCSGKVYYD LFEMRGSNSS IAIIRLEQLY
     PFEKKVVVEL LKKYNKASEF IWCQEEPMNM GAWRYITSHL NNALKEAGIN NEFKYIGREE
     SASPAVGSLQ AHNKQQEKLL KEALGVK
//