Sequence of DHAK_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
P76015
Escherichia coli (strain K12)
356
38215
Reaction
phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate
Other sequences found for EC No. 2.7.1.121
General information:
Sequence
0 MKKLINDVQD VLDEQLAGLA KAHPSLTLHQ DPVYVTRADA PVAGKVALLS GGGSGHEPMH
60 CGYIGQGMLS GACPGEIFTS PTPDKIFECA MQVDGGEGVL LIIKNYTGDI LNFETATELL
120 HDSGVKVTTV VIDDDVAVKD SLYTAGRRGV ANTVLIEKLV GAAAERGDSL DACAELGRKL
180 NNQGHSIGIA LGACTVPAAG KPSFTLADNE MEFGVGIHGE PGIDRRPFSS LDQTVDEMFD
240 TLLVNGSYHR TLRFWDYQQG SWQEEQQTKQ PLQSGDRVIA LVNNLGATPL SELYGVYNRL
300 TTRCQQAGLT IERNLIGAYC TSLDMTGFSI TLLKVDDETL ALWDAPVHTP ALNWGK
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in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
284236
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
284237
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
284238
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
284239
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
284240
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
284241
Siebold C.,Garcia-Alles L.F.,Erni B.,Baumann U.
A mechanism of covalent substrate binding in the X-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase.
Proc. Natl. Acad. Sci. U.S.A.
100
8188-8192
2003
284242
Garcia-Alles L.F.,Siebold C.,Luethi Nyffeler T.,Fluekiger-Bruehwiler K.,Schneider P.,Buergi H.-B.,Baumann U.,Erni B.
Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism.
Biochemistry
43
13037-13045
2004
284243
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
284244
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
