ID   ODO1_BUCAP              Reviewed;         923 AA.
AC   Q8K9N3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; OrderedLocusNames=BUsg_292;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67847.1; -; Genomic_DNA.
DR   RefSeq; NP_660636.1; -.
DR   GeneID; 1005496; -.
DR   GenomeReviews; AE013218_GR; BUsg_292.
DR   KEGG; bas:BUsg292; -.
DR   HOGENOM; Q8K9N3; -.
DR   OMA; Q8K9N3; QLAPFPW.
DR   BioCyc; BAPH198804:BUSG292-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    923       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162188.
SQ   SEQUENCE   923 AA;  107422 MW;  255A7653EED01A48 CRC64;
     MKKNTLEKWF NSSWLSGNNQ NYIEKIYESY LINPKSVDIT WQDKFSDLSK KRKNILKEEK
     FVYKNNSFKE IKIDKQEILE KKINYIINTF RKKGYKKSLI DPLKLNEQKK YKYLEPTFYH
     FSEDELKKTV KIDFKNSSQY EIKIRDLYEQ LNNKYCGSIG FEYMYIENSF EKKWITKHIE
     LFFKENLFIK KEKIRFLKEI LYGETFEKYL GKKFSGTKRF SLEGGETLIS ILHEIIRYSK
     KNDVSEIILG MAHRGRLNVL VNVLNKNPQV LFNEFSGINI PKEYSGDVKY HMGGITKIKN
     DKKKIYLKLA YNPSHLEIVN PVVLGIARAS INQLKISENK FLSINIHGDA SIIGQGVIQE
     TLNMSQTEAY KIGGTIHIVI NNQIGFTTSN PKNLRSSKYC TDVAKMIQAP VFHVNADDIE
     ASIFAIQLAL KFKKKFKKDV FIDLVCYRRH GHNEVDDPFV TQPIMYKKIH NHPTIGQIYS
     NLLISEKLIT SNDIEKIIEK YTTKLVQGKN VLSQERNITF QNGNKNFFIK KQKENTQLNF
     LNIKDLLYSI NTIPNSIEVH NRVKKIYQER IGMADGQILL DWGTAELLAY ATILKEGISC
     RLSGEDISRG TFFHRHAFIH DQNNGSIYVP LQNIEKNQGK FEIWDSVLSE EAVLAFEYGY
     SLFPSNNLTI WEAQFGDFAN GAQVVIDQFI SSSEQKWNQK SNLVLFLPHG YEGQGPEHSS
     ARLERFLQLC AENNIQVCIP TVSSQIFHLL RRQIFSNVYK PLIVLTPKSL LRNNVARSSL
     EVLVNENFKN VINEIDKNQK EVKRIIFCSG KIYYDLLEYR NKCDINNVLL IRIEQLYPFP
     KDEILTILKS YSYVQDFIWC QEEPHNQGAW FYIKDLLSTL LPLNSHLNYV SRPSAASPAA
     GHILIHRKEQ EKLINNAFNF KIA
//