ID   ODP1_BUCAP              Reviewed;         888 AA.
AC   Q8K9T9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=BUsg_199;
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 pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
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DR   EMBL; AE013218; AAM67763.1; -; Genomic_DNA.
DR   RefSeq; NP_660552.1; -.
DR   HSSP; P06958; 1L8A.
DR   SMR; Q8K9T9; 59-888.
DR   GeneID; 1005396; -.
DR   GenomeReviews; AE013218_GR; BUsg_199.
DR   KEGG; bas:BUsg199; -.
DR   HOGENOM; Q8K9T9; -.
DR   OMA; Q8K9T9; REISTTQ.
DR   BioCyc; BAPH198804:BUSG199-MON; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004660; 2-oxoA_DH_E1.
DR   InterPro; IPR005474; Transketo_N.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    888       Pyruvate dehydrogenase E1 component.
FT                                /FTId=PRO_0000162241.
SQ   SEQUENCE   888 AA;  101458 MW;  E127C03FB1261177 CRC64;
     MSEKLYNYDV DPVETNDWVQ SIESVIREEG LERAKFLIEK ILKKSKITRA NFFKCFFTSD
     YINTISSEEE VEYPGDLILE KRIRSAIRWN AIMMVLRASK KDLELGGHLS SFQSSATIYE
     VCFNHFFRSK NDEDGGDLVY FQGHIAPGIY ARSFLEGRLS KKQIDNFRQE VDGKGLSSYP
     HPKLMPNFWQ FPTVSMGLGP LCAIYQAKFL KYLQNRELKN TSKQTVYAFL GDGEMDEPES
     KGAISIAVRE KLDNLIFVIN CNLQRLDGPV VGNGKIVNEL ESFFYGAGWK VIKVIWGGKW
     DSLLKKDKTG KLIQLMNETI DGEYQTLKSK DGAYVRKYFF GKYQETLELV KNMTDEEIWN
     LNRGGHDPKK MFNALKKAKE IKDKPTVILA HTVKGYGMGV IAEGKNIAHQ IKKININGII
     YIRDRFNIPI SNEDIKELPY VVFEKNSKEY CYMHQQRKKL GGYIPFRLSK FTNALNIPDL
     IDFKSLLKEQ NKKMSTTIAF VRVLNLILKN HSIKNLIVPI IADEARTFGM EGLFRMIGIY
     SSIGQKYVPQ DREQLAYYKE EKKGQILQEG INELGAASSW LAAATSYSTN DFPMIPFYIY
     YSIFGFQRIG DLFWAAGDQQ ARGFLIGGTS GRTTLNGEGL QHEDGHSHIQ SLTIPNCVSY
     DPAFAYEVAV IIQDGLRRMY GPLQENIYYY ITTINENYYM PAMPQGVEKG ICKGIYKLKT
     FYATELKVQL MGSGAILRCI CKAGEILSND YCITTDIYSV TSFTELARNG EDCERWNMLH
     PYEKKRIAYI KTVMNSSPAV AATDYMKLFA EQIRHYIPSN EYHVLGTDGF GRSDSRDKLR
     DHFEVSAYYI VVAALNLLAK LNNINKKVVE EAIIKFNINA DKINPRLA
//