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InterPro: IPR005519 Acid phosphatase (Class B)

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UniProtKB

Matches:

660 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
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Accession

IPR005519 Acid_phosphat_B

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03767	Acid_phosphat_B	660
Signatures in BioMart

InterPro Relationships Help

Children

IPR006423 5-nucleotidase lipoprotein e(P4)
IPR010025 HAD-superfamily phosphatase, subfamily IIIB, AphA
IPR014403 Vegetative storage protein/acid phosphatase

GO Term annotation Help

Function

GO:0003993 acid phosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family of class B acid phosphatases also contains a number of vegetative storage proteins (VPS25). The acid phosphatase activity of VPS has been experimentally demonstrated [1].

Structural links Help

PDB - click here

SCOP: c.108.1.12

CATH: 3.40.50.1000

Database links Help

PANDIT: PF03767

Blocks: IPB005519

Pfam Clan: CL0137.11

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005519

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O04195 Uncharacterized protein At2g39920

P0AE22 Class B acid phosphatase

P10743 Stem 31 kDa glycoprotein

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010025	HAD-superfamily phosphatase, subfamily IIIB, AphA
IPR005519	Acid phosphatase (Class B)
IPR014403	Vegetative storage protein/acid phosphatase
IPR011267	Vegetative storage protein
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	DeWald DB, Mason HS, Mullet JE. The soybean vegetative storage proteins VSP alpha and VSP beta are acid phosphatases active on polyphosphates. J. Biol. Chem. 267 15958-64 1992 [PubMed: 1639823] http://intl.jbc.org/cgi/content/abstract/267/22/15958

Additional Reading Open in usermanual
	Makde RD, Kumar V, Gupta GD, Jasti J, Singh TP, Mahajan SK. Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium. Acta Crystallogr. D Biol. Crystallogr. 59 2003 1849-52 [PubMed: 14501135] http://dx.doi.org/10.1107/S0907444903018006
	Makde RD, Gupta GD, Mahajan SK, Kumar V. Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein. Arch. Biochem. Biophys. 464 2007 70-9 [PubMed: 17570338] http://dx.doi.org/10.1016/j.abb.2007.03.043
	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 2004 761-73 [PubMed: 14687572] http://dx.doi.org/10.1016/j.jmb.2003.10.050
	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. 355 2006 708-21 [PubMed: 16330049] http://dx.doi.org/10.1016/j.jmb.2005.10.068

InterPro 23.1