ID ODP1_ECO57 Reviewed; 887 AA. AC P0AFG9; P06958; P78049; Q53382; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 123. DE RecName: Full=Pyruvate dehydrogenase E1 component; DE Short=PDH E1 component; DE EC=1.2.4.1; GN Name=aceE; OrderedLocusNames=Z0124, ECs0118; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)- CC [(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2; CC Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10478, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005174; AAG54418.1; -; Genomic_DNA. DR EMBL; BA000007; BAB33541.1; -; Genomic_DNA. DR PIR; F85494; F85494. DR PIR; F90643; F90643. DR RefSeq; NP_308145.1; NC_002695.2. DR RefSeq; WP_000003820.1; NZ_AP018488.1. DR PDB; 3LPL; X-ray; 2.10 A; A/B=2-887. DR PDB; 3LQ2; X-ray; 1.96 A; A/B=2-887. DR PDB; 3LQ4; X-ray; 1.98 A; A/B=2-887. DR AlphaFoldDB; P0AFG9; -. DR MDRepo; P0AFG9; -. DR SMR; P0AFG9; -. DR IntAct; P0AFG9; 3. DR STRING; 155864.Z0124; -. DR GeneID; 75170013; -. DR GeneID; 75202071; -. DR GeneID; 913657; -. DR KEGG; ece:Z0124; -. DR KEGG; ecs:ECs_0118; -. DR PATRIC; fig|386585.9.peg.216; -. DR eggNOG; COG2609; Bacteria. DR HOGENOM; CLU_009154_2_0_6; -. DR OMA; WSVTSYK; -. DR EvolutionaryTrace; P0AFG9; -. DR Proteomes; UP000000558; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR CDD; cd02017; TPP_E1_EcPDC_like; 1. DR FunFam; 3.40.50.920:FF:000005; Pyruvate dehydrogenase E1 component; 1. DR FunFam; 3.40.50.970:FF:000009; Pyruvate dehydrogenase E1 component; 1. DR FunFam; 3.40.50.970:FF:000011; Pyruvate dehydrogenase E1 component; 1. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR035807; PDC_E1_N. DR InterPro; IPR051157; PDH/Transketolase. DR InterPro; IPR004660; PDH_E1. DR InterPro; IPR041621; PDH_E1_M. DR InterPro; IPR060495; PDH_E1_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR055152; Transketolase-like_C_2. DR InterPro; IPR005474; Transketolase_N. DR NCBIfam; TIGR00759; aceE; 1. DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1. DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1. DR Pfam; PF17831; PDH_E1_M; 1. DR Pfam; PF28598; PDH_E1_N; 1. DR Pfam; PF22613; Transketolase_C_1; 1. DR Pfam; PF00456; Transketolase_N; 1. DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR SUPFAM; SSF52922; TK C-terminal domain-like; 1. DR PDBsum; 3LPL; -. DR PDBsum; 3LQ2; -. DR PDBsum; 3LQ4; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Magnesium; Metal-binding; Oxidoreductase; KW Pyruvate; Reference proteome; Thiamine pyrophosphate. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..887 FT /note="Pyruvate dehydrogenase E1 component" FT /id="PRO_0000162244" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 716 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 76..99 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 109..124 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 197..214 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 243..248 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 275..285 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 300..305 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 310..317 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 320..326 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 331..337 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:3LQ4" FT HELIX 343..346 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 347..349 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 354..357 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 367..379 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 385..390 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 393..396 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 416..424 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 431..434 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 447..457 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 479..482 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 483..486 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 495..506 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 510..515 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 516..522 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 525..527 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 530..536 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 565..567 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 572..583 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 585..588 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 594..600 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 601..603 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 605..617 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 623..628 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 631..633 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 639..641 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 646..650 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 656..659 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 664..679 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 687..691 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 700..703 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 707..712 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 714..720 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 726..731 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 733..735 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 736..750 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 753..760 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 762..778 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 783..785 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 788..792 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 798..801 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 807..810 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 813..815 FT /evidence="ECO:0007829|PDB:3LQ2" FT STRAND 817..819 FT /evidence="ECO:0007829|PDB:3LQ4" FT STRAND 821..824 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 835..841 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 846..860 FT /evidence="ECO:0007829|PDB:3LQ2" FT HELIX 865..874 FT /evidence="ECO:0007829|PDB:3LQ2" FT TURN 884..886 FT /evidence="ECO:0007829|PDB:3LQ2" SQ SEQUENCE 887 AA; 99668 MW; 7FB3811DE11BDD02 CRC64; MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA //