ID   ODP1_BUCBP              Reviewed;         887 AA.
AC   Q89AR0;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=bbp_189;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26921.1; -; Genomic_DNA.
DR   RefSeq; WP_011091322.1; NC_004545.1.
DR   AlphaFoldDB; Q89AR0; -.
DR   SMR; Q89AR0; -.
DR   STRING; 224915.bbp_189; -.
DR   PRIDE; Q89AR0; -.
DR   EnsemblBacteria; AAO26921; AAO26921; bbp_189.
DR   GeneID; 56470731; -.
DR   KEGG; bab:bbp_189; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_6; -.
DR   OMA; PDEYRTF; -.
DR   OrthoDB; 49937at2; -.
DR   Proteomes; UP000000601; 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; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..887
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000162242"
SQ   SEQUENCE   887 AA;  100906 MW;  89A9A18649A6A78A CRC64;
     MAEFSSNDID PIETEDWIQA IKSVIREDGL ERANFIINTV KKYVPYKNKV VFKKCAISNY
     VNTIPVEEEP NYPGDLFIEQ KIRSVIRWNA IMMVLRASKK NLDLGGHLSS FQSAATIYEV
     CFNHFFHATN ENNGGDLVYF QGHISPGIYS RAFIEDRLTQ KQLDNFRQEI DGIGLSSYPH
     PKLMPNFWQF PTVSMGLGPI CAIYQAKFLK YLEHRNLKCT NNQKVYAFLG DGEMDEPESK
     GAISIAAREK LDNLIFIVNC NLQRLDGPVI GNGKVIDELE SVFKGCGWKV IKVIWGSKWD
     SLLKKDVSGK LIKLMNETLD GDYQTFKSKN GAYIRKYFFG KYLETQELVK DMSDDQIWNL
     DRGGHDPKKI YAALSKANSI VGKPVIILMH TVKGYGMGDI AEGKNIAHQI KKIDIKGITY
     IKNRFKVPVE ENELKYLPYV SFDANSIEYK YLHARRKKLG GYLPIRLSNF TNFFTLPKLD
     EFSTLLTEQK KEISTTIVFI RILNILLRNS FIKDRIVPII ADEARTFGME GLFRKIGIYN
     FIGQKYTPQD KELLAYYKED KKGQILQEGI NELGAAASWL AAATSYSTNN FPMIPFYIFY
     SMFGFQRIGD LFWAAGDQQA RGFLIGGTSG KTTLNGEGLQ HGDGHSHIQA LTIPNCISYN
     PAYAYELAVI VHDGLQRMYG PSQENIYYYI TTMNENYVMP GISKNMYEGI CKGIYKLKHV
     GKKNVKVQIM GSGSILQCVC RAAEILLEEY DIGSDVYSVT SFTELARNGQ DCDRWNLLHP
     TQEKKVPFVT KIMNKLPAIA VTDYMKLFSE QVRAYIPAVT YRVLGTDGFG RSDSRKNLRR
     YFEIDEYHIV IAVLGELEKI GDVDKNTIVN AISKFKIDIN KVNPRLA