Sequence of KPRS_ECOLI
EC Number:2.7.6.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Other sequences found for EC No. 2.7.6.1
General information:
Sequence
0 MPDMKLFAGN ATPELAQRIA NRLYTSLGDA AVGRFSDGEV SVQINENVRG GDIFIIQSTC
60 APTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR VRSARVPITA KVVADFLSSV
120 GVDRVLTVDL HAEQIQGFFD VPVDNVFGSP ILLEDMLQLN LDNPIVVSPD IGGVVRARAI
180 AKLLNDTDMA IIDKRRPRAN VSQVMHIIGD VAGRDCVLVD DMIDTGGTLC KAAEALKERG
240 AKRVFAYATH PIFSGNAANN LRNSVIDEVV VCDTIPLSDE IKSLPNVRTL TLSGMLAEAI
300 RRISNEESIS AMFEH
Download this sequence
in fasta formatDownload all sequences for 2.7.6.1
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1206017
Hove-Jensen B.,Harlow K.W.,King C.J.,Switzer R.L.
Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene.
J. Biol. Chem.
261
6765-6771
1986
1206018
Bower S.G.,Harlow K.W.,Switzer R.L.,Hove-Jensen B.
Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site.
J. Biol. Chem.
264
10287-10291
1989
1206019
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
1206020
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
1206021
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
1206022
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
1206023
Hove-Jensen B.,Nygaard P.
Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification of a mutant enzyme.
Eur. J. Biochem.
126
327-332
1982
1206024
Hilden I.,Hove-Jensen B.,Harlow K.W.
Inactivation of Escherichia coli phosphoribosylpyrophosphate synthetase by the 2',3'-dialdehyde derivative of ATP. Identification of active site lysines.
J. Biol. Chem.
270
20730-20736
1995
1206025
Willemoes M.,Nilsson D.,Hove-Jensen B.
Effects of mutagenesis of aspartic acid residues in the putative phosphoribosyl diphosphate binding site of Escherichia coli phosphoribosyl diphosphate synthetase on metal ion specificity and ribose 5-phosphate binding.
Biochemistry
35
8181-8186
1996
1206026
Willemoes M.,Hove-Jensen B.
Binding of divalent magnesium by Escherichia coli phosphoribosyl diphosphate synthetase.
Biochemistry
36
5078-5083
1997
1206027
Willemoes M.,Hove-Jensen B.,Larsen S.
Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase.
J. Biol. Chem.
275
35408-35412
2000
1206028
Hove-Jensen B.,Andersen K.R.,Kilstrup M.,Martinussen J.,Switzer R.L.,Willemoes M.
Phosphoribosyl diphosphate (PRPP): biosynthesis, enzymology, utilization, and metabolic significance.
Microbiol. Mol. Biol. Rev.
81
0-0
2017
