Conserved Site

Sulfatase, conserved site (IPR024607)

Short name: Sulfatase_CS

Description

Sulphatases EC:3.1.6. are enzymes that hydrolyze various sulphate esters. The sequence of different types of sulphatases are available and have shown to be structurally related [PMID: 2303452, PMID: 2122463, PMID: 2476654]; these include:

  • arylsulphatase A EC:3.1.6.8 (ASA), a lysosomal enzyme which hydrolyses cerebroside sulphate;
  • arylsulphatase B EC:3.1.6.12 (ASB), which hydrolyses the sulphate ester group from N-acetylgalactosamine 4-sulphate residues of dermatan sulphate;
  • arylsulphatase C (ASD) and E (ASE);
  • steryl-sulphatase EC:3.1.6.2 (STS), a membrane bound microsomal enzyme which hydrolyses 3-beta-hydroxy steroid sulphates;
  • iduronate 2-sulphatase precursor EC:3.1.6.13 (IDS), a lysosomal enzyme that hydrolyses the 2-sulphate groups from non-reducing-terminal iduronic acid residues in dermatan sulphate and heparan sulphate;
  • N-acetylgalactosamine-6-sulphatase EC:3.1.6.4, which hydrolyses the 6-sulphate groups of the N-acetyl-d-galactosamine 6-sulphate units of chondroitin sulphate and the D-galactose 6-sulphate units of keratan sulphate;
  • glucosamine-6-sulphatase EC:3.1.6.14 (G6S), which hydrolyses the N-acetyl-D-glucosamine 6-sulphate units of heparan sulphate and keratan sulphate;
  • N-sulphoglucosamine sulphohydrolase EC:3.10.1.1 (sulphamidase), the lysosomal enzyme that catalyses the hydrolysis of N-sulpho-d-glucosamine into glucosamine and sulphate;
  • sea urchin embryo arylsulphatase EC:3.1.6.1;
  • green algae arylsulphatase EC:3.1.6.1, which plays an important role in the mineralisation of sulphates;
  • and arylsulphatase EC:3.1.6.1 from Escherichia coli (aslA), Klebsiella aerogenes (gene atsA) and Pseudomonas aeruginosa (gene atsA).

This entry represents two conserved sites for the sulphatase family located in the N-terminal region. The SULPHATASE_1 site contains the conserved arginine which could be implicated in the catalytic mechanism; it is located four residues after a position that, in eukaryotic sulphatases, is a conserved cysteine which has been shown [PMID: 8681943] to be modified to 2-amino-3-oxopropionic acid. In prokaryotes, this cysteine is replaced by a serine.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE patterns