{PDOC00117} {PS00523; SULFATASE_1} {PS00149; SULFATASE_2} {BEGIN} ************************* * Sulfatases signatures * ************************* Sulfatases (EC 3.1.6.-) are enzymes that hydrolyze various sulfate esters. The sequence of different types of sulfatases are available. These enzymes are: - Arylsulfatase A (EC 3.1.6.8) (ASA), a lysosomal enzyme which hydrolyzes cerebroside sulfate. - Arylsulfatase B (EC 3.1.6.12) (ASB), a lysosomal enzyme which hydrolyzes the sulfate ester group from N-acetylgalactosamine 4-sulfate residues of dermatan sulfate. - Arylsulfatase C (ASD). - Arylsulfatase E (ASE). - Steryl-sulfatase (EC 3.1.6.2) (STS) (arylsulfatase C), a membrane bound microsomal enzyme which hydrolyzes 3-beta-hydroxy steroid sulfates. - Iduronate 2-sulfatase precursor (EC 3.1.6.13) (IDS), a lysosomal enzyme that hydrolyzes the 2-sulfate groups from non-reducing-terminal iduronic acid residues in dermatan sulfate and heparan sulfate. - N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4), an enzyme that hydrolyzes the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and the D-galactose 6-sulfate units of keratan sulfate. - Choline sulfatase (EC 3.1.6.6) (gene betC), a bacterial enzyme that converts choline-O-sulfate to choline. - Glucosamine-6-sulfatase (EC 3.1.6.14) (G6S), a lysosomal enzyme that hydrolyzes the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. - N-sulphoglucosamine sulphohydrolase (EC 3.10.1.1) (sulphamidase), the lysosomal enzyme that catalyzes the hydrolysis of N-sulfo-d-glucosamine into glucosamine and sulfate. - Sea urchin embryo arylsulfatase (EC 3.1.6.1). - Green alga arylsulfatase (EC 3.1.6.1), an enzyme which plays an important role in the mineralization of sulfates. - Arylsulfatase (EC 3.1.6.1) from Escherichia coli (gene aslA), Klebsiella aerogenes (gene atsA) and Pseudomonas aeruginosa (gene atsA). - Escherichia coli hypothetical protein yidJ. It has been shown that all these sulfatases are structurally related [1,2,3]. As signature patterns for that family of enzymes we have selected the two best conserved regions. Both regions are located in the N-terminal section of these enzymes. The first region contains a conserved arginine which could be implicated in the catalytic mechanism; it is located four residues after a position that, in eukaryotic sulfatases, is a conserved cysteine which has been shown [4] to be modified to 2-amino-3-oxopropionic acid. In prokaryotes, this cysteine is replaced by a serine. -Consensus pattern: [SAPG]-[LIVMST]-[CS]-[STACG]-P-[STA]-R-x(2)-[LIVMFW](2)- [TAR]-G [R is a putative active site residue] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: G-[YV]-x-[ST]-x(2)-[IVAS]-G-K-x(0,1)-[FYWMK]-[HL] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuhlsdorf M., Vingron M., Meyer H.E., Pohlmann R., von Figura K. "Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B." J. Biol. Chem. 265:3374-3381(1990). PubMed=2303452 [ 2] Wilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J., Clements P.R., Hopwood J.J. "Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA." Proc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990). PubMed=2122463 [ 3] de Hostos E.L., Schilling J., Grossman A.R. Mol. Gen. Genet. 218:229-239(1989). [ 4] Selmer T., Hallmann A., Schmidt B., Sumper M., von Figura K. "The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri." Eur. J. Biochem. 238:341-345(1996). PubMed=8681943 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}