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   03-AUG-2022, entry version 121.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=BUsg_199;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   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: Component of the pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of multiple
CC       copies of pyruvate dehydrogenase (E1), dihydrolipoamide
CC       acetyltransferase (E2) and lipoamide dehydrogenase (E3). {ECO:0000250}.
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DR   EMBL; AE013218; AAM67763.1; -; Genomic_DNA.
DR   RefSeq; WP_011053730.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9T9; -.
DR   SMR; Q8K9T9; -.
DR   STRING; 198804.BUsg_199; -.
DR   PRIDE; Q8K9T9; -.
DR   EnsemblBacteria; AAM67763; AAM67763; BUsg_199.
DR   KEGG; bas:BUsg_199; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_6; -.
DR   OMA; PDEYRTF; -.
DR   OrthoDB; 49937at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           1..888
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="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