ID   ODP1_BUCAI              Reviewed;         887 AA.
AC   P57301;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=BU205;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB12922.1; -; Genomic_DNA.
DR   RefSeq; NP_240036.1; NC_002528.1.
DR   RefSeq; WP_010896002.1; NC_002528.1.
DR   AlphaFoldDB; P57301; -.
DR   SMR; P57301; -.
DR   STRING; 107806.10038887; -.
DR   PRIDE; P57301; -.
DR   EnsemblBacteria; BAB12922; BAB12922; BAB12922.
DR   KEGG; buc:BU205; -.
DR   PATRIC; fig|107806.10.peg.216; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_6; -.
DR   OMA; PDEYRTF; -.
DR   Proteomes; UP000001806; 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_0000162240"
SQ   SEQUENCE   887 AA;  101396 MW;  B6AB82C012826105 CRC64;
     MSENLYNDVD PIETRDWVQA IESVIRREGH KRAHFLIEQV LKTAKINRKE FFRSSFTSDY
     INTISREDEY EYPGNLILEK RIRSAIRWNA IMMVLRASKK NLELGGHLSS FQSSATIYEV
     CFNHFFQAKN HKDGGDLVYF QGHISPGIYA RSFLEGRLSE EQIDNFRQEV DGIGLSSYPH
     PKLMPNFWQF PTVSMGLGPL CAIYQAKFLK YLHNRELKNT SKQIVYAFLG DGEMDEPESK
     GAISIAVREK LDNLIFIINC NLQRLDGPVV GNGKIVNELE SFFYGAGWKV IKVIWGSRWD
     CLLKKDTSGK LIQLMNETVD GDYQTFKSKD GAYVRKYFFG KYKETYDLVK DMTDEEIWKL
     NRGGHDPKKM FNALKKAKET KYKPTVILAH TVKGYGMGVI AEGKNIAHQI KKININGIIH
     IRDRFNIPVS NDEINKLPYV TFKKNSEEYC YIHSQRKKLG GYIPFRLSSF TGKLILPKLI
     DFQSLLEEQK KDISTTVAFI RVLNIILKNN SIKHLIVPII ADEARTFGME GLFRKIGIYS
     SSGQKYTPQD REQLAYYKEE KKGQILQEGI NELGAASSWL AAATSYSTND FPMILFYIYY
     SIFGFQRIGD LFWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
     PAFAYEVAVI IQDGLRRMYG PSQENIYYYI TTINENYYMP AMPIGVEEGI CKGIYKLKTL
     HGTTSKVQLI GSGAILRSVC EAAEILLKDY SITTDIYSVT SFTELARNGE DCERWNMLHP
     NEKNKIAYVK QIMNKNPTVA ATDYMKLFAE QIRHYIPSQE YHVLGTDGFG RSDSRDKLRD
     HFEVNAYYIV IAALNLLANI NDIKKKVVED AIMKFNIDAN KINPRLS