Home ScanProsite ProRule Documents Downloads Links Funding
PROSITE documentation PDOC00117

Sulfatases signatures

Description:

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-β-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.

Last update:

December 2004 / Pattern and text revised.

Technical section:

PROSITE methods (with tools and information) covered by this documentation:

SULFATASE_1, PS00523; Sulfatases signature 1  (PATTERN)
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.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00523
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00523
• Scan Swiss-Prot/TrEMBL entries against PS00523
• view ligand binding statistics
Matching PDB structures: 1E1Z 1E3C [ALL]
SULFATASE_2, PS00149; Sulfatases signature 2  (PATTERN)
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.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00149
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00149
• Scan Swiss-Prot/TrEMBL entries against PS00149
• view ligand binding statistics
Matching PDB structures: 1AUK 1E1Z 1E2S 1E33 ... [ALL]

References:

1 AuthorsPeters C., Schmidt B., Rommerskirch W., Rupp K., Zuhlsdorf M., Vingron M., Meyer H.E., Pohlmann R., von Figura K.
TitlePhylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B.
SourceJ. Biol. Chem. 265:3374-3381(1990).
PubMed ID2303452
2 AuthorsWilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J., Clements P.R., Hopwood J.J.
TitleHunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA.
SourceProc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990).
PubMed ID2122463
3 Authorsde Hostos E.L., Schilling J., Grossman A.R.
SourceMol. Gen. Genet. 218:229-239(1989).
4 AuthorsSelmer T., Hallmann A., Schmidt B., Sumper M., von Figura K.
TitleThe evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri.
SourceEur. J. Biochem. 238:341-345(1996).
PubMed ID8681943

Copyright:

PROSITE is copyright. It is produced by the Swiss Institute of Bioinformatics (SIB). There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to license@isb-sib.ch or see: http://www.expasy.org/prosite/prosite_license.htm.

Miscellaneous:

View entry in original PROSITE document format
View entry in raw text format (no links)