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 27-MAR-2024, entry version 114.
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; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC 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=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; 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=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}.
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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_002695.1.
DR RefSeq; WP_000003820.1; NZ_VOAI01000002.1.
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 PDBsum; 3LPL; -.
DR PDBsum; 3LQ2; -.
DR PDBsum; 3LQ4; -.
DR AlphaFoldDB; P0AFG9; -.
DR SMR; P0AFG9; -.
DR IntAct; P0AFG9; 3.
DR STRING; 155864.Z0124; -.
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; PDEYRTF; -.
DR EvolutionaryTrace; P0AFG9; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.970; -; 2.
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 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; 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.
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 76..99
FT /evidence="ECO:0007829|PDB:3LQ2"
FT HELIX 109..124
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 447..457
FT /evidence="ECO:0007829|PDB:3LQ2"
FT TURN 458..460
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 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 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 811..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..859
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
//
