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Sequence of APHA_ECOLI

EC Number:3.1.3.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
acid phosphatase
P0AE22
Escherichia coli (strain K12)
237
26104
Reaction
a phosphate monoester + H2O = an alcohol + phosphate
Other sequences found for EC No. 3.1.3.2

General information:

Sequence
show sequence in fasta format
  0 MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS VAQIENSLAG
 60 RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV FWEKMNNGWD EFSIPKEVAR
120 QLIDMHVRRG DAIFFVTGRS PTKTETVSKT LADNFHIPAT NMNPVIFAGD KPGQNTKSQW
180 LQDKNIRIFY GDSDNDITAA RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
132242
Thaller M.C.,Schippa S.,Bonci A.,Cresti S.,Rossolini G.M.
Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product.
FEMS Microbiol. Lett.
146
191-198
1997
132243
Blattner F.R.,Burland V.D.,Plunkett G. III,Sofia H.J.,Daniels D.L.
Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.
Nucleic Acids Res.
21
5408-5417
1993
132244
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
132245
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
132246
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
132247
Forleo C.,Benvenuti M.,Calderone V.,Schippa S.,Docquier J.D.,Thaller M.C.,Rossolini G.M.,Mangani S.
Expression, purification, crystallization and preliminary X-ray characterization of the class B acid phosphatase (AphA) from Escherichia coli.
Acta Crystallogr. D
59
1058-1060
2003
132248
Passariello C.,Forleo C.,Micheli V.,Schippa S.,Leone R.,Mangani S.,Thaller M.C.,Rossolini G.M.
Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655.
Biochim. Biophys. Acta
1764
13-19
2006
132249
Calderone V.,Forleo C.,Benvenuti M.,Cristina Thaller M.,Maria Rossolini G.,Mangani S.
The first structure of a bacterial class B acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.
J. Mol. Biol.
335
761-773
2004
132250
Calderone V.,Forleo C.,Benvenuti M.,Thaller M.C.,Rossolini G.M.,Mangani S.
A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.
J. Mol. Biol.
355
708-721
2006
132251
Leone R.,Cappelletti E.,Benvenuti M.,Lentini G.,Thaller M.C.,Mangani S.
Structural insights into the catalytic mechanism of the bacterial class B phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.
J. Mol. Biol.
384
478-488
2008