Class B acid phosphatase
Details
- Name
- Class B acid phosphatase
- Kind
- protein
- Synonyms
- 3.1.3.2
- CBAP
- napA
- yjbP
- Gene Name
- aphA
- UniProtKB Entry
- P0AE22Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsacid phosphatase activity / cofactor binding / metal ion binding / phosphoserine phosphatase activityProcessesdephosphorylationComponentsouter membrane-bounded periplasmic space
- General 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.
- Specific Function
- acid phosphatase activity
- Pfam Domain Function
- Acid_phosphat_B (PF03767)
- Signal Regions
- 1-25
- 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
Resource Link UniProtKB ID P0AE22 UniProtKB Entry Name APHA_ECOLI GenBank Protein ID 1256442 GenBank Gene ID U51210 PDB ID(s) 1N8N, 1N9K, 1RMQ, 1RMT, 1RMY, 2B82, 2B8J, 2G1A, 2HEG, 2HF7, 3CZ4 KEGG ID ecj:JW4015 NCBI Gene ID 948562 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2'-Deoxycytidine experimental, investigational unknown target Details