Sulfatase, conserved site
IPR024607
Definition
Sulphatases [ec:3.1.6.] are enzymes that hydrolyse various sulphate esters. The sequence of different types of sulphatases are available and have shown to be structurally related [[cite:PMID:2303452], [cite:PMID:2122463], [cite: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.
16 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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