Identification
Name:Class B acid phosphatase
Synonyms:Not Available
Gene Name:aphA
Enzyme Class:
Biological Properties
General Function:Involved in acid phosphatase activity
Specific Function:Dephosphorylates several organic phosphomonoesters and catalyzes the transfer of low-energy phosphate groups from phosphomonoesters to hydroxyl groups of various organic compounds. Preferentially acts on aryl phosphoesters. Might function as a broad-spectrum dephosphorylating enzyme able to scavenge both 3'- and 5'-nucleotides and also additional organic phosphomonoesters
Cellular Location:Periplasm (Potential)
SMPDB Pathways:
KEGG Pathways:
  • 1,4-Dichlorobenzene degradation ec00627
  • Microbial metabolism in diverse environments ec01120
  • Riboflavin metabolism ec00740
  • gamma-Hexachlorocyclohexane degradation ec00361
KEGG Reactions:
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SMPDB Reactions:
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EcoCyc Reactions:
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Complex Reactions:
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A phosphate monoester+Thumban alcohol+Thumb
A phosphate monoester + Water → an alcohol + Inorganic phosphate
ReactionCard
A phosphate monoester+Thumban alcohol+Thumb
A phosphate monoester + Water → an alcohol + Inorganic phosphate
ReactionCard
A phosphate monoester+Thumban alcohol+Thumb
A phosphate monoester + Water → an alcohol + Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB010442'-Deoxyguanosine 5'-monophosphateMetaboCard
ECMDB012324-NitrophenolMetaboCard
ECMDB012275-Thymidylic acidMetaboCard
ECMDB00050AdenosineMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00089CytidineMetaboCard
ECMDB00095Cytidine monophosphateMetaboCard
ECMDB02033D-Ribose-5-phosphateMetaboCard
ECMDB01202dCMPMetaboCard
ECMDB00101DeoxyadenosineMetaboCard
ECMDB00905Deoxyadenosine monophosphateMetaboCard
ECMDB00014DeoxycytidineMetaboCard
ECMDB00085DeoxyguanosineMetaboCard
ECMDB00071DeoxyinosineMetaboCard
ECMDB00012DeoxyuridineMetaboCard
ECMDB06555DIMPMetaboCard
ECMDB01409dUMPMetaboCard
ECMDB01520Flavin MononucleotideMetaboCard
ECMDB00131GlycerolMetaboCard
ECMDB21222Glycerol 2-phosphateMetaboCard
ECMDB00133GuanosineMetaboCard
ECMDB01397Guanosine monophosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00195InosineMetaboCard
ECMDB04085Inosinic acidMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00167L-ThreonineMetaboCard
ECMDB21238L-Threonine O-3-phosphateMetaboCard
ECMDB00158L-TyrosineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00272PhosphoserineMetaboCard
ECMDB21276PhosphotyrosineMetaboCard
ECMDB00244RiboflavinMetaboCard
ECMDB00283RiboseMetaboCard
ECMDB00273ThymidineMetaboCard
ECMDB00296UridineMetaboCard
ECMDB00288Uridine 5'-monophosphateMetaboCard
ECMDB00494WaterMetaboCard
ECMDB00299XanthosineMetaboCard
ECMDB01554Xanthylic acidMetaboCard
GO Classification:
Component
cell part
outer membrane-bounded periplasmic space
periplasmic space
Function
acid phosphatase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphatase activity
phosphoric ester hydrolase activity
Gene Properties
Blattner:b4055
Gene OrientationClockwise
Centisome Percentage:91.98
Left Sequence End4267437
Right Sequence End4268150
Gene Sequence:
>714 bp
ATGGAATCATACTCGCAAAACAGCAATAAATTAGATTTTCAGCACGAGGCCAGGATATTA
AACGGTATATGGCTCATTACCGCTTTAGGTTTGGTGGCAACCGCAGGACTAGCCTGGGGA
GCTAAGTATATCGAAATTACGGCAACCAAATATGATTCACCACCAATGTATGTCGCCATA
GGGTTATTATTACTTTGTATGTATGGCTTAAGTAAGGATATCAACAAGATAAATGCCGCC
ATCGCGGGCGTAATATATCTGTTTTTACTCTCTTTGGTGGCGATTGTCGTTGCAAGTTTA
GTTCCTGTATATGCCATTATCATCGTGTTCAGCACTGCGGGCGCGATGTTTTTAATCAGT
ATGCTGGCCGGTTTATTATTTAATGTTGATCCTGGTTCTCACCGTTTTATCATTATGATG
ACGTTGACAGGGTTGGCCCTGGTAATCATCGTGAATGCGGCATTAATGAGTGAACGGCCC
ATTTGGATAATAAGTTGCTTAATGATTGTGTTATGGTCAGGCATTATCTCGCATGGACGA
AATAAGCTCCTTGAATTGGCGGGGAAATGCCATAGTGAAGAGTTGTGGAGTCCGGTTCGT
TGCGCTTTTACAGGTGCATTAACACTCTATTACTATTTTATCGGCTTCTTTGGGATACTT
GCCGCGATAGCTATAACGCTTGTCTGGCAAAGGCATACGCGTTTTTTTCATTAG
Protein Properties
Pfam Domain Function:
Protein Residues:237
Protein Molecular Weight:26103
Protein Theoretical pI:8
PDB File:1N9K
Signaling Regions:
  • 1-25
Transmembrane Regions:
  • None
Protein Sequence:
>Class B acid phosphatase
MRKITQAISAVCLLFALNSSAVALASSPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAG
RPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVAR
QLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQW
LQDKNIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY
References
External Links:
ResourceLink
Uniprot ID:P0AE22
Uniprot Name:APHA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062344
PDB ID:1N9K
Ecogene ID:EG11934
Ecocyc:EG11934
ColiBase:b4055
Kegg Gene:b4055
EchoBASE ID:EB1878
CCDB:APHA_ECOLI
BacMap:16131881
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "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. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Calderone, V., Forleo, C., Benvenuti, M., Cristina Thaller, M., Maria Rossolini, G., Mangani, S. (2004). "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. Pubmed: 14687572
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Thaller, M. C., Schippa, S., Bonci, A., Cresti, S., Rossolini, G. M. (1997). "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. Pubmed: 9011040