Class B acid phosphatase

Details

Name
Class B acid phosphatase
Synonyms
  • 3.1.3.2
  • CBAP
  • napA
  • yjbP
Gene Name
aphA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0003993|Class B acid phosphatase
MRKITQAISAVCLLFALNSSAVALASSPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAG
RPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVAR
QLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQW
LQDKNIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY
Number of residues
237
Molecular Weight
26103.29
Theoretical pI
7.6
GO Classification
Functions
acid phosphatase activity / cofactor binding / metal ion binding / phosphoserine phosphatase activity
Processes
dephosphorylation
Components
outer membrane-bounded periplasmic space
General Function
Phosphoserine phosphatase activity
Specific Function
Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0021312|Class B acid phosphatase (aphA)
ATGCGCAAGATCACACAGGCAATCAGTGCCGTTTGCTTATTGTTCGCTCTAAACAGTTCC
GCTGTTGCCCTGGCCTCATCTCCTTCACCGCTTAACCCTGGGACTAACGTTGCCAGGCTT
GCTGAACAGGCACCCATTCATTGGGTTTCGGTCGCACAAATTGAAAATAGCCTCGCAGGG
CGTCCGCCAATGGCGGTGGGGTTTGATATCGATGACACGGTACTTTTTTCCAGTCCGGGC
TTCTGGCGCGGCAAAAAAACCTTCTCGCCAGAAAGCGAAGATTATCTGAAAAATCCTGTG
TTCTGGGAAAAAATGAACAATGGCTGGGATGAATTCAGCATTCCAAAAGAGGTCGCTCGC
CAGCTGATTGATATGCATGTACGCCGCGGTGACGCGATCTTCTTTGTGACTGGTCGTAGC
CCGACGAAAACAGAAACGGTTTCAAAAACGCTGGCGGATAATTTTCATATTCCTGCCACC
AACATGAATCCGGTGATCTTTGCGGGCGATAAACCAGGGCAAAATACAAAATCGCAATGG
CTGCAGGATAAAAATATCCGAATTTTTTATGGCGATTCTGATAATGATATTACCGCCGCA
CGCGATGTCGGCGCTCGTGGTATCCGCATTCTGCGCGCCTCCAACTCTACCTACAAACCC
TTGCCACAAGCGGGTGCGTTTGGTGAAGAGGTGATCGTCAATTCAGAATACTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AE22
UniProtKB Entry NameAPHA_ECOLI
GenBank Protein ID1256442
GenBank Gene IDU51210
General References
  1. Thaller MC, Schippa S, Bonci A, Cresti S, Rossolini GM: Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product. FEMS Microbiol Lett. 1997 Jan 15;146(2):191-8. [Article]
  2. Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  6. Forleo C, Benvenuti M, Calderone V, Schippa S, Docquier JD, Thaller MC, Rossolini GM, Mangani S: Expression, purification, crystallization and preliminary X-ray characterization of the class B acid phosphatase (AphA) from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1058-60. Epub 2003 May 23. [Article]
  7. Passariello C, Forleo C, Micheli V, Schippa S, Leone R, Mangani S, Thaller MC, Rossolini GM: Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655. Biochim Biophys Acta. 2006 Jan;1764(1):13-9. Epub 2005 Nov 2. [Article]
  8. Calderone V, Forleo C, Benvenuti M, Cristina Thaller M, Rossolini GM, 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. 2004 Jan 16;335(3):761-73. [Article]
  9. Calderone V, Forleo C, Benvenuti M, Thaller MC, Rossolini GM, 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. 2006 Jan 27;355(4):708-21. Epub 2005 Nov 10. [Article]
  10. Leone R, Cappelletti E, Benvenuti M, Lentini G, Thaller MC, 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. 2008 Dec 12;384(2):478-88. doi: 10.1016/j.jmb.2008.09.050. Epub 2008 Sep 27. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB025942'-Deoxycytidineexperimental, investigationalunknownDetails