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InterPro: IPR017849 Alkaline phosphatase-like, alpha/beta/alpha

Protein matches Help

UniProtKB

Matches:

10214 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

Accession

IPR017849 Alkaline_Pase-like_a/b/a

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.720.10	Alk_phosphtse	10214
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000917 Sulfatase
IPR001952 Alkaline phosphatase
IPR002591 Type I phosphodiesterase/nucleotide pyrophosphatase/phosphate transferase
IPR005995 Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent
IPR007070 GPI ethanolamine phosphate transferase 1
IPR012083 Arylsulfatase, plant
IPR012159 Membrane sulfatase, HI0842-related
IPR012160 Membrane sulfatase, HI1246-related
IPR012251 N-acetylglucosamine-6-sulfatase
IPR012710 Phosphonoacetate hydrolase
IPR014615 Extracellular sulfatase
IPR015981 N-acetylglucosamine-6-sulfatase, eukaryotic
IPR017785 Choline-sulfatase
IPR017850 Alkaline-phosphatase-like, core domain
IPR020881 Phosphoglycerol transferase I

Contains

IPR006124 Metalloenzyme
IPR018299 Alkaline phosphatase, active site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a structural domain with a 3-layer alpha/beta/alpha structure that forms the core domain of alkaline phosphatases. These enzymes can have several large insertions, but these extra subdomains are not covered by this entry. This structural domain is found in:

Alkaline phosphatase (EC:3.1.3.1); most use zinc and magnesium as cofactors [1, 2].
Arylsulphatase (has an additional C-terminal alpha+beta subdomain) (EC:3.1.6.8) [3, 4].
Phosphoglycerate mutase (catalytic domain) (EC:5.4.2.1) [5].
Phosphonoacetate hydrolase (contains an alpha+beta subdomain inserted near C terminus) (EC:3.11.1.2); uses zinc as a cofactor.

Structural links Help

PDB - click here

SCOP: c.76.1.1 , c.76.1.2 , c.76.1.3 , c.76.1.4

CATH: 1.10.287.550 , 3.30.1120.10 , 3.30.1360.110 , 3.40.720.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017849

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P05187 Alkaline phosphatase, placental type

P06802 Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

P11491 Repressible alkaline phosphatase

P90754 Ectonucleotide pyrophosphatase/phosphodiesterase C27A7.1

Q24238 Alkaline phosphatase 4

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020821	Extracellular Endonuclease, subunit A
IPR017849	Alkaline phosphatase-like, alpha/beta/alpha
IPR020436	Somatomedin B, chordata
IPR018299	Alkaline phosphatase, active site
IPR002591	Type I phosphodiesterase/nucleotide pyrophosphatase/phosphate transferase
IPR001604	DNA/RNA non-specific endonuclease
IPR001952	Alkaline phosphatase
IPR017850	Alkaline-phosphatase-like, core domain
IPR001212	Somatomedin B
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Wang J, Stieglitz KA, Kantrowitz ER. Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase. Biochemistry 44 8378-86 2005 [PubMed: 15938627] http://dx.doi.org/10.1021/bi050155p
2.	Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J. Mol. Biol. 350 441-51 2005 [PubMed: 15946677] http://dx.doi.org/10.1016/j.jmb.2005.04.068
3.	Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W. Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry 37 3654-64 1998 [PubMed: 9521684] http://dx.doi.org/10.1021/bi9714924
4.	Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D. Structure of human estrone sulfatase suggests functional roles of membrane association. J. Biol. Chem. 278 22989-97 2003 [PubMed: 12657638] http://dx.doi.org/10.1074/jbc.M211497200
5.	Rigden DJ, Lamani E, Mello LV, Littlejohn JE, Jedrzejas MJ. Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling. J. Mol. Biol. 328 909-20 2003 [PubMed: 12729763] http://dx.doi.org/10.1016/S0022-2836(03)00350-4

Additional Reading Open in usermanual
	de Backer MM, McSweeney S, Lindley PF, Hough E. Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 1555-61 [PubMed: 15333925] http://dx.doi.org/10.1107/S0907444904015628
	Wang J, Kantrowitz ER. Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine. Protein Sci. 15 2006 2395-401 [PubMed: 17008720] http://dx.doi.org/10.1110/ps.062351506
	Llinas P, Masella M, Stigbrand T, Menez A, Stura EA, Le Du MH. Structural studies of human alkaline phosphatase in complex with strontium: implication for its secondary effect in bones. Protein Sci. 15 2006 1691-700 [PubMed: 16815919] http://dx.doi.org/10.1110/ps.062123806

InterPro 23.1