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InterPro: IPR011158 Nonspecific acid phosphatase, class A
Protein matches
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UniProtKB Matches: 104 proteins |
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Accession
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IPR011158 Acid_Pase_ClassA |
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Type
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Signatures
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InterPro Relationships
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Parent
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IPR001011 Acid phosphatase, class A, bacterial
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Contains
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IPR016118 Phosphatidic acid phosphatase/chloroperoxidase, N-terminal
IPR018296 Acid phosphatase, class A, bacterial, conserved site
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GO Term annotation
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Function
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GO:0003993 acid phosphatase activity
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Component
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GO:0030288 outer membrane-bounded periplasmic space
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This group represents nonspecific acid phosphatases, class A [1, 2]. Non-specific acid phosphatases are bacterial enzymes that catalyse the dephosphorylation of orthophosphoric monoesters to alcohol and phosphate, in addition to being able to catalyse transphosphorylation. As their name suggests, they show broad specificity, being able to phosphorylate a wide range of hydroxy compounds. During active catalysis, an activated phospho-enzyme intermediate is formed that is able to transfer its phosphate group to water, glucose or inosine. Nonspecific acid phosphatases share a conserved active site with mammalian glucose-6-phosphatases (G6Pase) [3].
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Structural links
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Database links
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Publications
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1.
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Uchiya KI, Tohsuji M, Nikai T, Sugihara H, Sasakawa C.
Identification and characterization of phoN-Sf, a gene on the large plasmid of Shigella flexneri 2a encoding a nonspecific phosphatase.
J. Bacteriol. 178 4548-54 1996
[PubMed: 8755883]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8755883
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2.
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Thaller MC, Berlutti F, Schippa S, Lombardi G, Rossolini GM.
Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii.
Microbiology (Reading, Engl.) 140 ( Pt 6) 1341-50 1994
[PubMed: 8081499]
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3.
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Tanaka N, Hasan Z, Hartog AF, van Herk T, Wever R, Sanders RJ.
Phosphorylation and dephosphorylation of polyhydroxy compounds by class A bacterial acid phosphatases.
Org. Biomol. Chem. 1 2833-9 2003
[PubMed: 12968332]
http://dx.doi.org/10.1039/b304012g
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Additional Reading
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Makde RD, Kumar V, Rao AS, Yadava VS, Mahajan SK.
Purification, crystallization and preliminary X-ray diffraction studies of recombinant class A non-specific acid phosphatase of Salmonella typhimurium.
Acta Crystallogr. D Biol. Crystallogr. 59 2003 515-8
[PubMed: 12595712]
http://dx.doi.org/10.1107/S0907444902022679
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Makde RD, Mahajan SK, Kumar V.
Structure and mutational analysis of the PhoN protein of Salmonella typhimurium provide insight into mechanistic details.
Biochemistry 46 2007 2079-90
[PubMed: 17263560]
http://dx.doi.org/10.1021/bi062180g
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Ishikawa K, Mihara Y, Gondoh K, Suzuki E, Asano Y.
X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.
EMBO J. 19 2000 2412-23
[PubMed: 10835340]
http://dx.doi.org/10.1093/emboj/19.11.2412
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Makde RD, Dikshit K, Kumar V.
Protein engineering of class-A non-specific acid phosphatase (PhoN) of Salmonella typhimurium: modulation of the pH-activity profile.
Biomol. Eng. 23 2006 247-51
[PubMed: 16901752]
http://dx.doi.org/10.1016/j.bioeng.2006.06.004
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Ishikawa K, Mihara Y, Shimba N, Ohtsu N, Kawasaki H, Suzuki E, Asano Y.
Enhancement of nucleoside phosphorylation activity in an acid phosphatase.
Protein Eng. 15 2002 539-43
[PubMed: 12200535]
http://dx.doi.org/10.1093/protein/15.7.539
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InterPro 23.1
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