ODP1_ECOLI
ID ODP1_ECOLI Reviewed; 887 AA.
AC P0AFG8; P06958; P78049; Q53382;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pyruvate dehydrogenase E1 component;
DE Short=PDH E1 component;
DE EC=1.2.4.1;
GN Name=aceE; OrderedLocusNames=b0114, JW0110;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6343085; DOI=10.1111/j.1432-1033.1983.tb07441.x;
RA Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.;
RT "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide
RT sequence encoding the pyruvate dehydrogenase component.";
RL Eur. J. Biochem. 133:155-162(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 145
RP AND 275.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=K12;
RX PubMed=8262214; DOI=10.1016/0014-5793(93)81605-y;
RA Haydon D.J., Quail M.A., Guest J.R.;
RT "A mutation causing constitutive synthesis of the pyruvate dehydrogenase
RT complex in Escherichia coli is located within the pdhR gene.";
RL FEBS Lett. 336:43-47(1993).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=11955070; DOI=10.1021/bi0118557;
RA Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y.,
RA Jordan F., Guest J.R., Furey W.;
RT "Structure of the pyruvate dehydrogenase multienzyme complex E1 component
RT from Escherichia coli at 1.85 A resolution.";
RL Biochemistry 41:5213-5221(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 -!- 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
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).
CC -!- INTERACTION:
CC P0AFG8; P0AFG8: aceE; NbExp=2; IntAct=EBI-542683, EBI-542683;
CC P0AFG8; P0A8N7: epmA; NbExp=2; IntAct=EBI-542683, EBI-562598;
CC P0AFG8; P77439: fryA; NbExp=2; IntAct=EBI-542683, EBI-545399;
CC P0AFG8; P46889: ftsK; NbExp=2; IntAct=EBI-542683, EBI-550795;
CC P0AFG8; P0A6F5: groEL; NbExp=3; IntAct=EBI-542683, EBI-543750;
CC P0AFG8; P0AEV9: hycI; NbExp=2; IntAct=EBI-542683, EBI-552628;
CC P0AFG8; P0AB83: nth; NbExp=3; IntAct=EBI-542683, EBI-555213;
CC P0AFG8; P0AB89: purB; NbExp=2; IntAct=EBI-542683, EBI-556534;
CC P0AFG8; P0AG40: ribF; NbExp=2; IntAct=EBI-542683, EBI-542969;
CC P0AFG8; P05100: tag; NbExp=2; IntAct=EBI-542683, EBI-558722;
CC P0AFG8; P26602: ubiC; NbExp=2; IntAct=EBI-542683, EBI-559360;
CC P0AFG8; P0A9U1: ybhF; NbExp=3; IntAct=EBI-542683, EBI-547696;
CC P0AFG8; P0A8L7: yciU; NbExp=3; IntAct=EBI-542683, EBI-544511;
CC P0AFG8; P76049: ycjY; NbExp=2; IntAct=EBI-542683, EBI-544654;
CC P0AFG8; P76170: ynfB; NbExp=2; IntAct=EBI-542683, EBI-544774;
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; V01498; CAA24740.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73225.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96684.2; -; Genomic_DNA.
DR EMBL; S67363; AAB29357.1; -; Genomic_DNA.
DR PIR; B64734; DEECPV.
DR RefSeq; NP_414656.1; NC_000913.3.
DR RefSeq; WP_000003820.1; NZ_STEB01000010.1.
DR PDB; 1L8A; X-ray; 1.85 A; A/B=2-887.
DR PDB; 1RP7; X-ray; 2.09 A; A/B=2-887.
DR PDB; 2G25; X-ray; 2.10 A; A/B=2-887.
DR PDB; 2G28; X-ray; 1.85 A; A/B=2-887.
DR PDB; 2G67; X-ray; 2.32 A; A/B=2-887.
DR PDB; 2IEA; X-ray; 1.85 A; A/B=2-887.
DR PDB; 2QTA; X-ray; 1.85 A; A/B=2-887.
DR PDB; 2QTC; X-ray; 1.77 A; A/B=2-887.
DR PDBsum; 1L8A; -.
DR PDBsum; 1RP7; -.
DR PDBsum; 2G25; -.
DR PDBsum; 2G28; -.
DR PDBsum; 2G67; -.
DR PDBsum; 2IEA; -.
DR PDBsum; 2QTA; -.
DR PDBsum; 2QTC; -.
DR AlphaFoldDB; P0AFG8; -.
DR SMR; P0AFG8; -.
DR BioGRID; 4261303; 14.
DR BioGRID; 849234; 1.
DR ComplexPortal; CPX-3943; Pyruvate dehydrogenase complex.
DR DIP; DIP-9039N; -.
DR IntAct; P0AFG8; 104.
DR STRING; 511145.b0114; -.
DR DrugBank; DB01987; Cocarboxylase.
DR CarbonylDB; P0AFG8; -.
DR iPTMnet; P0AFG8; -.
DR SWISS-2DPAGE; P0AFG8; -.
DR jPOST; P0AFG8; -.
DR PaxDb; P0AFG8; -.
DR PRIDE; P0AFG8; -.
DR EnsemblBacteria; AAC73225; AAC73225; b0114.
DR EnsemblBacteria; BAB96684; BAB96684; BAB96684.
DR GeneID; 66671598; -.
DR GeneID; 944834; -.
DR KEGG; ecj:JW0110; -.
DR KEGG; eco:b0114; -.
DR PATRIC; fig|1411691.4.peg.2168; -.
DR EchoBASE; EB0023; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_6; -.
DR InParanoid; P0AFG8; -.
DR OMA; PDEYRTF; -.
DR PhylomeDB; P0AFG8; -.
DR BioCyc; EcoCyc:E1P-MON; -.
DR BioCyc; MetaCyc:E1P-MON; -.
DR BRENDA; 1.2.1.104; 2026.
DR BRENDA; 1.2.4.1; 2026.
DR SABIO-RK; P0AFG8; -.
DR EvolutionaryTrace; P0AFG8; -.
DR PRO; PR:P0AFG8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0045250; C:cytosolic pyruvate dehydrogenase complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IC:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0004738; F:pyruvate dehydrogenase activity; IGI:EcoliWiki.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:CAFA.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0042867; P:pyruvate catabolic process; IC:ComplexPortal.
DR CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR DisProt; DP00427; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Glycolysis;
KW Magnesium; Metal-binding; Oxidoreductase; Pyruvate; Reference proteome;
KW Thiamine pyrophosphate.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..887
FT /note="Pyruvate dehydrogenase E1 component"
FT /id="PRO_0000162243"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 716
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 146
FT /note="P -> R (in Ref. 1; CAA24740)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="Missing (in Ref. 1; CAA24740)"
FT /evidence="ECO:0000305"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 197..214
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1L8A"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 347..351
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:2QTA"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:2G25"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:2G25"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 495..506
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 510..515
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 516..522
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 549..552
FT /evidence="ECO:0007829|PDB:2G25"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:2G25"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 572..583
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 594..600
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 605..617
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 631..633
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 646..650
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 664..679
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 687..691
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:1L8A"
FT HELIX 707..712
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 715..720
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 723..731
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 736..750
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 752..758
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 762..778
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 788..792
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 798..801
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 807..810
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 811..815
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 817..819
FT /evidence="ECO:0007829|PDB:2QTA"
FT STRAND 821..824
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 835..841
FT /evidence="ECO:0007829|PDB:2QTC"
FT HELIX 846..859
FT /evidence="ECO:0007829|PDB:2QTC"
FT STRAND 861..863
FT /evidence="ECO:0007829|PDB:2G67"
FT HELIX 865..874
FT /evidence="ECO:0007829|PDB:2QTC"
FT TURN 884..886
FT /evidence="ECO:0007829|PDB:2QTC"
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
