Sequence of PPB_ECOLI
EC Number:3.1.3.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a phosphate monoester + H2O = an alcohol + phosphate
Other sequences found for EC No. 3.1.3.1
General information:
Sequence
0 MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD QTAALRDSLS
60 DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY
120 VTDSAASATA WSTGVKTYNG ALGVDIHEKD HPTILEMAKA AGLATGNVST AELQDATPAA
180 LVAHVTSRKC YGPSATSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG
240 EWQGKTLREQ AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN
300 IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ
360 IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA PDTKAPGLTQ ALNTKDGAVM
420 VMSYGNSEED SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
461291
Shuttleworth H.,Taylor J.,Minton N.
Sequence of the gene for alkaline phosphatase from Escherichia coli JM83.
Nucleic Acids Res.
14
8689-8689
1986
461292
Chang C.N.,Kuang W.-J.,Chen E.Y.
Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli.
Gene
44
121-125
1986
461293
Dubose R.F.,Dykhuizen D.E.,Hartl D.L.
Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli.
Proc. Natl. Acad. Sci. U.S.A.
85
7036-7040
1988
461295
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
461296
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
461297
Agrawal D.K.,Wanner B.L.
A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase.
J. Bacteriol.
172
3180-3190
1990
461298
Kikuchi Y.,Yoda K.,Yamasaki M.,Tamura G.
The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli.
Nucleic Acids Res.
9
5671-5678
1981
461299
Bradshaw R.A.,Cancedda F.,Ericsson L.H.,Neumann P.A.,Piccoli S.P.,Schlesinger M.J.,Shriefer K.,Walsh K.A.
Amino acid sequence of Escherichia coli alkaline phosphatase.
Proc. Natl. Acad. Sci. U.S.A.
78
3473-3477
1981
461300
Inouye H.,Barnes W.,Beckwith J.
Signal sequence of alkaline phosphatase of Escherichia coli.
J. Bacteriol.
149
434-439
1982
461301
Laforet G.A.,Kaiser E.T.,Kendall D.A.
Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli.
J. Biol. Chem.
264
14478-14485
1989
461302
Gray G.L.,Baldridge J.S.,McKeown K.S.,Heyneker H.L.,Chang C.N.
Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable.
Gene
39
247-254
1985
461303
Michaelis S.,Hunt J.F.,Beckwith J.
Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli.
J. Bacteriol.
167
160-167
1986
461304
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
461305
Sowadski J.M.,Handschumacher M.D.,Krishna Murthy H.M.,Foster B.A.,Wyckoff H.W.
Refined structure of alkaline phosphatase from Escherichia coli at 2.8-A resolution.
J. Mol. Biol.
186
417-433
1985
461306
Kim E.E.,Wyckoff H.W.
Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis.
J. Mol. Biol.
218
449-464
1991
461307
Dealwis C.G.,Brennan C.,Christianson K.,Mandecki W.,Abad-Zapatero C.
Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase.
Biochemistry
34
13967-13973
1995
461308
Ma L.,Kantrowitz E.R.
Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites.
Biochemistry
35
2394-2402
1996
461309
Murphy J.E.,Stec B.,Ma L.,Kantrowitz E.R.
Trapping and visualization of a covalent enzyme-phosphate intermediate.
Nat. Struct. Biol.
4
618-622
1997
461310
Stec B.,Hehir M.J.,Brennan C.,Nolte M.,Kantrowitz E.R.
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.
J. Mol. Biol.
277
647-662
1998
461311
Holtz K.M.,Stec B.,Kantrowitz E.R.
A model of the transition state in the alkaline phosphatase reaction.
J. Biol. Chem.
274
8351-8354
1999
461312
Saio T.,Guan X.,Rossi P.,Economou A.,Kalodimos C.G.
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Science
344
1250494-1250494
2014
