Sequence of DHAL_ECOLI
EC Number:2.7
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 2.7
EC Number:2.7.1.29
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + glycerone = ADP + glycerone phosphate
Other sequences found for EC No. 2.7.1.29
EC Number:2.7.1.121
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
phosphoenolpyruvate-glycerone phosphotransferase
P76014
Escherichia coli (strain K12)
210
22632
Reaction
phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate
Other sequences found for EC No. 2.7.1.121
General information:
Sequence
0 MSLSRTQIVN WLTRCGDIFS TESEYLTGLD REIGDADHGL NMNRGFSKVV EKLPAIADKD
60 IGFILKNTGM TLLSSVGGAS GPLFGTFFIR AAQATQARQS LTLEELYQMF RDGADGVISR
120 GKAEPGDKTM CDVWVPVVES LRQSSEQNLS VPVALEAASS IAESAAQSTI TMQARKGRAS
180 YLGERSIGHQ DPGATSVMFM MQMLALAAKE
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
284251
Oshima T.,Aiba H.,Baba T.,Fujita K.,Hayashi K.,Honjo A.,Ikemoto K.,Inada T.,Itoh T.,Kajihara M.,Kanai K.,Kashimoto K.,Kimura S.,Kitagawa M.,Makino K.,Masuda S.,Miki T.,Mizobuchi K.,Mori H.,Motomura K.,Nakamura Y.,Nashimoto H.,Nishio Y.,Saito N.,Sampei G.,Seki Y.,Tagami H.,Takemoto K.,Wada C.,Yamamoto Y.,Yano M.,Horiuchi T.
A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.
DNA Res.
3
137-155
1996
284252
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
284253
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
0-0
2006
284254
Fountoulakis M.,Takacs M.-F.,Berndt P.,Langen H.,Takacs B.
Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography.
Electrophoresis
20
2181-2195
1999
284255
Gutknecht R.,Beutler R.,Garcia-Alles L.F.,Baumann U.,Erni B.
The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor.
EMBO J.
20
2480-2486
2001
284256
Baechler C.,Fluekiger-Bruehwiler K.,Schneider P.,Baehler P.,Erni B.
From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases.
J. Biol. Chem.
280
18321-18325
2005
284257
Baechler C.,Schneider P.,Baehler P.,Lustig A.,Erni B.
Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR.
EMBO J.
24
283-293
2005
284258
Oberholzer A.E.,Schneider P.,Baumann U.,Erni B.
Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase.
J. Mol. Biol.
359
539-545
2006
284259
Shi R.,McDonald L.,Cui Q.,Matte A.,Cygler M.,Ekiel I.
Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase.
Proc. Natl. Acad. Sci. U.S.A.
108
1302-1307
2011
284260
Shi R.,McDonald L.,Cygler M.,Ekiel I.
Coiled-coil helix rotation selects repressing or activating state of transcriptional regulator DhaR.
Structure
22
478-487
2014
