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Pyruvate dehydrogenase E1 component (PDH E1 component) (EC 1.2.4.1)

 ODP1_ECOLI              Reviewed;         887 AA.
P0AFG8; P06958; P78049; Q53382;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 128.
RecName: Full=Pyruvate dehydrogenase E1 component;
Short=PDH E1 component;
EC=1.2.4.1;
Name=aceE; OrderedLocusNames=b0114, JW0110;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6343085; DOI=10.1111/j.1432-1033.1983.tb07441.x;
Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.;
"The pyruvate dehydrogenase complex of Escherichia coli K12.
Nucleotide sequence encoding the pyruvate dehydrogenase component.";
Eur. J. Biochem. 133:155-162(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8202364; DOI=10.1093/nar/22.9.1637;
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
TO 145 AND 275.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
STRAIN=K12;
PubMed=8262214; DOI=10.1016/0014-5793(93)81605-Y;
Haydon D.J., Quail M.A., Guest J.R.;
"A mutation causing constitutive synthesis of the pyruvate
dehydrogenase complex in Escherichia coli is located within the pdhR
gene.";
FEBS Lett. 336:43-47(1993).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
PubMed=11955070; DOI=10.1021/bi0118557;
Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M.,
Yan Y., Jordan F., Guest J.R., Furey W.;
"Structure of the pyruvate dehydrogenase multienzyme complex E1
component from Escherichia coli at 1.85 A resolution.";
Biochemistry 41:5213-5221(2002).
-!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex,
that catalyzes the overall conversion of pyruvate to acetyl-CoA
and CO(2).
-!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
-!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of
multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide
acetyltransferase (E2) and lipoamide dehydrogenase (E3).
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-542683, EBI-542683;
P0A8N7:epmA; NbExp=2; IntAct=EBI-542683, EBI-562598;
P77439:fryA; NbExp=2; IntAct=EBI-542683, EBI-545399;
P46889:ftsK; NbExp=2; IntAct=EBI-542683, EBI-550795;
P0A6F5:groL; NbExp=3; IntAct=EBI-542683, EBI-543750;
P0AEV9:hycI; NbExp=2; IntAct=EBI-542683, EBI-552628;
P0AB83:nth; NbExp=3; IntAct=EBI-542683, EBI-555213;
P0AB89:purB; NbExp=2; IntAct=EBI-542683, EBI-556534;
P0AG40:ribF; NbExp=2; IntAct=EBI-542683, EBI-542969;
P05100:tag; NbExp=2; IntAct=EBI-542683, EBI-558722;
P26602:ubiC; NbExp=2; IntAct=EBI-542683, EBI-559360;
P0A9U1:ybhF; NbExp=3; IntAct=EBI-542683, EBI-547696;
P0A8L7:yciU; NbExp=3; IntAct=EBI-542683, EBI-544511;
P76049:ycjY; NbExp=2; IntAct=EBI-542683, EBI-544654;
P76170:ynfB; NbExp=2; IntAct=EBI-542683, EBI-544774;
-----------------------------------------------------------------------
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EMBL; V01498; CAA24740.1; -; Genomic_DNA.
EMBL; U00096; AAC73225.1; -; Genomic_DNA.
EMBL; AP009048; BAB96684.2; -; Genomic_DNA.
EMBL; S67363; AAB29357.1; -; Genomic_DNA.
PIR; B64734; DEECPV.
RefSeq; NP_414656.1; NC_000913.3.
RefSeq; WP_000003820.1; NZ_LN832404.1.
PDB; 1L8A; X-ray; 1.85 A; A/B=2-887.
PDB; 1RP7; X-ray; 2.09 A; A/B=2-887.
PDB; 2G25; X-ray; 2.10 A; A/B=2-887.
PDB; 2G28; X-ray; 1.85 A; A/B=2-887.
PDB; 2G67; X-ray; 2.32 A; A/B=2-887.
PDB; 2IEA; X-ray; 1.85 A; A/B=2-887.
PDB; 2QTA; X-ray; 1.85 A; A/B=2-887.
PDB; 2QTC; X-ray; 1.77 A; A/B=2-887.
PDBsum; 1L8A; -.
PDBsum; 1RP7; -.
PDBsum; 2G25; -.
PDBsum; 2G28; -.
PDBsum; 2G67; -.
PDBsum; 2IEA; -.
PDBsum; 2QTA; -.
PDBsum; 2QTC; -.
DisProt; DP00427; -.
ProteinModelPortal; P0AFG8; -.
SMR; P0AFG8; -.
BioGrid; 4261303; 14.
BioGrid; 849234; 1.
DIP; DIP-9039N; -.
IntAct; P0AFG8; 104.
STRING; 316385.ECDH10B_0094; -.
DrugBank; DB01987; Thiamin Diphosphate.
CarbonylDB; P0AFG8; -.
iPTMnet; P0AFG8; -.
SWISS-2DPAGE; P0AFG8; -.
EPD; P0AFG8; -.
PaxDb; P0AFG8; -.
PRIDE; P0AFG8; -.
EnsemblBacteria; AAC73225; AAC73225; b0114.
EnsemblBacteria; BAB96684; BAB96684; BAB96684.
GeneID; 944834; -.
KEGG; ecj:JW0110; -.
KEGG; eco:b0114; -.
PATRIC; fig|1411691.4.peg.2168; -.
EchoBASE; EB0023; -.
EcoGene; EG10024; aceE.
eggNOG; ENOG4105DAQ; Bacteria.
eggNOG; COG2609; LUCA.
HOGENOM; HOG000115215; -.
InParanoid; P0AFG8; -.
KO; K00163; -.
OMA; REPWFPG; -.
PhylomeDB; P0AFG8; -.
BioCyc; EcoCyc:E1P-MONOMER; -.
BioCyc; MetaCyc:E1P-MONOMER; -.
BRENDA; 1.2.4.1; 2026.
SABIO-RK; P0AFG8; -.
EvolutionaryTrace; P0AFG8; -.
PRO; PR:P0AFG8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
GO; GO:0004738; F:pyruvate dehydrogenase activity; IGI:EcoliWiki.
GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:CAFA.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
CDD; cd02017; TPP_E1_EcPDC_like; 1.
Gene3D; 3.40.50.920; -; 1.
InterPro; IPR004660; 2-oxoA_DH_E1.
InterPro; IPR035807; PDC_E1_N.
InterPro; IPR029061; THDP-binding.
InterPro; IPR009014; Transketo_C/PFOR_II.
InterPro; IPR005474; Transketolase_N.
PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
Pfam; PF00456; Transketolase_N; 1.
PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
SUPFAM; SSF52518; SSF52518; 2.
SUPFAM; SSF52922; SSF52922; 1.
TIGRFAMs; TIGR00759; aceE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Glycolysis; Magnesium; Metal-binding;
Oxidoreductase; Pyruvate; Reference proteome; Thiamine pyrophosphate.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298646}.
CHAIN 2 887 Pyruvate dehydrogenase E1 component.
/FTId=PRO_0000162243.
METAL 231 231 Magnesium.
METAL 261 261 Magnesium.
METAL 263 263 Magnesium; via carbonyl oxygen.
MOD_RES 716 716 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
CONFLICT 146 146 P -> R (in Ref. 1; CAA24740).
{ECO:0000305}.
CONFLICT 276 276 Missing (in Ref. 1; CAA24740).
{ECO:0000305}.
HELIX 66 68 {ECO:0000244|PDB:2QTC}.
HELIX 76 99 {ECO:0000244|PDB:2QTC}.
HELIX 109 124 {ECO:0000244|PDB:2QTC}.
STRAND 131 133 {ECO:0000244|PDB:2QTC}.
STRAND 137 139 {ECO:0000244|PDB:2QTC}.
HELIX 142 144 {ECO:0000244|PDB:2QTC}.
HELIX 145 154 {ECO:0000244|PDB:2QTC}.
HELIX 160 163 {ECO:0000244|PDB:2QTC}.
TURN 181 183 {ECO:0000244|PDB:2QTC}.
TURN 185 187 {ECO:0000244|PDB:2QTC}.
HELIX 197 214 {ECO:0000244|PDB:2QTC}.
STRAND 225 230 {ECO:0000244|PDB:2QTC}.
HELIX 232 235 {ECO:0000244|PDB:2QTC}.
HELIX 237 240 {ECO:0000244|PDB:2QTC}.
HELIX 243 248 {ECO:0000244|PDB:2QTC}.
STRAND 254 260 {ECO:0000244|PDB:2QTC}.
STRAND 262 264 {ECO:0000244|PDB:1L8A}.
STRAND 265 269 {ECO:0000244|PDB:2QTC}.
HELIX 275 285 {ECO:0000244|PDB:2QTC}.
STRAND 289 293 {ECO:0000244|PDB:2QTC}.
HELIX 299 305 {ECO:0000244|PDB:2QTC}.
HELIX 310 317 {ECO:0000244|PDB:2QTC}.
HELIX 320 326 {ECO:0000244|PDB:2QTC}.
HELIX 331 337 {ECO:0000244|PDB:2QTC}.
STRAND 339 342 {ECO:0000244|PDB:2QTC}.
HELIX 343 346 {ECO:0000244|PDB:2QTC}.
TURN 347 351 {ECO:0000244|PDB:2QTC}.
HELIX 354 358 {ECO:0000244|PDB:2QTC}.
HELIX 363 365 {ECO:0000244|PDB:2QTC}.
HELIX 367 379 {ECO:0000244|PDB:2QTC}.
STRAND 385 390 {ECO:0000244|PDB:2QTC}.
TURN 393 396 {ECO:0000244|PDB:2QTC}.
TURN 398 400 {ECO:0000244|PDB:2QTA}.
TURN 401 403 {ECO:0000244|PDB:2G25}.
HELIX 407 409 {ECO:0000244|PDB:2G25}.
HELIX 416 424 {ECO:0000244|PDB:2QTC}.
HELIX 431 434 {ECO:0000244|PDB:2QTC}.
HELIX 447 458 {ECO:0000244|PDB:2QTC}.
HELIX 479 482 {ECO:0000244|PDB:2QTC}.
HELIX 483 486 {ECO:0000244|PDB:2QTC}.
HELIX 495 506 {ECO:0000244|PDB:2QTC}.
TURN 510 515 {ECO:0000244|PDB:2QTC}.
STRAND 516 522 {ECO:0000244|PDB:2QTC}.
HELIX 525 527 {ECO:0000244|PDB:2QTC}.
HELIX 530 536 {ECO:0000244|PDB:2QTC}.
TURN 549 552 {ECO:0000244|PDB:2G25}.
STRAND 553 555 {ECO:0000244|PDB:2G25}.
STRAND 565 567 {ECO:0000244|PDB:2QTC}.
HELIX 572 583 {ECO:0000244|PDB:2QTC}.
HELIX 585 588 {ECO:0000244|PDB:2QTC}.
STRAND 594 600 {ECO:0000244|PDB:2QTC}.
HELIX 601 603 {ECO:0000244|PDB:2QTC}.
HELIX 605 617 {ECO:0000244|PDB:2QTC}.
STRAND 623 628 {ECO:0000244|PDB:2QTC}.
TURN 631 633 {ECO:0000244|PDB:2QTC}.
TURN 635 637 {ECO:0000244|PDB:2QTC}.
TURN 639 641 {ECO:0000244|PDB:2QTC}.
HELIX 646 650 {ECO:0000244|PDB:2QTC}.
STRAND 656 659 {ECO:0000244|PDB:2QTC}.
HELIX 664 679 {ECO:0000244|PDB:2QTC}.
STRAND 687 691 {ECO:0000244|PDB:2QTC}.
TURN 704 706 {ECO:0000244|PDB:1L8A}.
HELIX 707 712 {ECO:0000244|PDB:2QTC}.
STRAND 715 720 {ECO:0000244|PDB:2QTC}.
STRAND 723 731 {ECO:0000244|PDB:2QTC}.
HELIX 733 735 {ECO:0000244|PDB:2QTC}.
HELIX 736 750 {ECO:0000244|PDB:2QTC}.
STRAND 752 758 {ECO:0000244|PDB:2QTC}.
HELIX 762 778 {ECO:0000244|PDB:2QTC}.
HELIX 788 792 {ECO:0000244|PDB:2QTC}.
STRAND 798 801 {ECO:0000244|PDB:2QTC}.
HELIX 807 810 {ECO:0000244|PDB:2QTC}.
HELIX 811 815 {ECO:0000244|PDB:2QTC}.
STRAND 817 819 {ECO:0000244|PDB:2QTA}.
STRAND 821 824 {ECO:0000244|PDB:2QTC}.
HELIX 835 841 {ECO:0000244|PDB:2QTC}.
HELIX 846 859 {ECO:0000244|PDB:2QTC}.
STRAND 861 863 {ECO:0000244|PDB:2G67}.
HELIX 865 874 {ECO:0000244|PDB:2QTC}.
TURN 884 886 {ECO:0000244|PDB:2QTC}.
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


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