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InterPro: IPR016274 Histidine acid phosphatase, eukaryotic

UniProtKB

Matches:

233 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
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
Matches in BioMart

IPR016274 Histidine_acid_Pase_euk

Type

Family

Signatures Help

Parent

IPR000560 Histidine acid phosphatase

InterPro annotation

This group represents euakaryotic histidine acid phosphatases.

SCOP: c.60.1.2

CATH: 3.40.50.1240

Enzyme: EC:3.1.3

IPR016274

Numbers of overlapping proteins

Average numbers of overlapping amino acids

O00092 3-phytase A

O35217 Multiple inositol polyphosphate phosphatase 1

P00635 Repressible acid phosphatase

Q9UNW1 Multiple inositol polyphosphate phosphatase 1

Q9Z2L6 Multiple inositol polyphosphate phosphatase 1

InterPro entry accession number/name and structure databases		Colour code
IPR016274	Histidine acid phosphatase, eukaryotic
IPR000560	Histidine acid phosphatase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Additional Reading Open in usermanual
	Kostrewa D, Wyss M, D'Arcy A, van Loon AP. Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution. J. Mol. Biol. 288 1999 965-74 [PubMed: 10329192] http://dx.doi.org/10.1006/jmbi.1999.2736
	Xiang T, Liu Q, Deacon AM, Koshy M, Kriksunov IA, Lei XG, Hao Q, Thiel DJ. Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine. J. Mol. Biol. 339 2004 437-45 [PubMed: 15136045] http://dx.doi.org/10.1016/j.jmb.2004.03.057
	Liu Q, Huang Q, Lei XG, Hao Q. Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics. Structure 12 2004 1575-83 [PubMed: 15341723] http://dx.doi.org/10.1016/j.str.2004.06.015
	Kostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP. Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution. Nat. Struct. Biol. 4 1997 185-90 [PubMed: 9164457] http://dx.doi.org/10.1038/nsb0397-185

InterPro 24.0