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26  structures 3819  species 1  interaction 18763  sequences 130  architectures

Family: Sulfatase (PF00884)

Summary: Sulfatase

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Sulfatase Edit Wikipedia article

1p49 opm.gif
Identifiers
Symbol Sulfatase
Pfam PF00884
InterPro IPR000917
PROSITE PDOC00117
SCOP 1auk
SUPERFAMILY 1auk
OPM superfamily 24
OPM protein 1p49

Sulfatases EC 3.1.6. are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates.

Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfate esters.

Occurrence and importance[edit]

Sulfatases are found in lower and higher organisms. In higher organisms they are found in intracellular and extracellular spaces. Steroid sulfatase is distributed in a wide range of tissues throughout the body, enabling sulfated steroids synthesized in the adrenals and gonads to be desulfated following distribution through the circulation system. A large number of sulfatases are localized in the lysosome, an acidic digestive organelle found within the cell. Lysosomal sulfatases cleave a range of sulfated carbohydrates including sulfated glycosaminoglycans and glycolipids. Genetic defects in sulfatase activity can arise through mutations in individual sulfatases and result in certain lysosomal storage disorders with a spectrum of phenotypes ranging from defects in physical and intellectual development.

Three-dimensional structure[edit]

The following sulfatases have been shown to be structurally related based on their sequence homology:[1][2][3]

Human proteins containing this domain[edit]

ARSA; ARSB; ARSD; ARSE; ARSF; ARSG; ARSH; ARSI; ARSJ; ARSK; GALNS; GNS; IDS; PIGG; SGSH; STS; SULF1; SULF2;

References[edit]

  1. ^ von Figura K, Vingron M, Schmidt B, Meyer HE, Peters C, Rommerskirch W, Rupp K, Pohlmann R, Zuhlsdorf M (1990). "Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B". J. Biol. Chem. 265 (6): 3374–3381. PMID 2303452. 
  2. ^ Wilson PJ, Morris CP, Anson DS, Occhiodoro T, Bielicki J, Clements PR, Hopwood JJ (1990). "Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA". Proc. Natl. Acad. Sci. U.S.A. 87 (21): 8531–8535. doi:10.1073/pnas.87.21.8531. PMC 54990. PMID 2122463. 
  3. ^ Grossman AR, de Hostos EL, Schilling J (1989). "Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii". Mol. Gen. Genet. 218 (2): 229–239. doi:10.1007/BF00331273. PMID 2476654. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR000917

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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Literature references

  1. Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W; , Biochemistry 1998;37:3654-3664.: 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. PUBMED:9521684 EPMC:9521684


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000917

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

  • arylsulphatase A EC (ASA), a lysosomal enzyme which hydrolyses cerebroside sulphate;
  • arylsulphatase B EC (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 (STS), a membrane bound microsomal enzyme which hydrolyses 3-beta-hydroxy steroid sulphates;
  • iduronate 2-sulphatase precursor EC (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, 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 (G6S), which hydrolyses the N-acetyl-D-glucosamine 6-sulphate units of heparan sulphate and keratan sulphate;
  • N-sulphoglucosamine sulphohydrolase EC (sulphamidase), the lysosomal enzyme that catalyses the hydrolysis of N-sulpho-d-glucosamine into glucosamine and sulphate;
  • sea urchin embryo arylsulphatase EC;
  • green algae arylsulphatase EC, which plays an important role in the mineralisation of sulphates;
  • and arylsulphatase EC from Escherichia coli (aslA), Klebsiella aerogenes (gene atsA) and Pseudomonas aeruginosa (gene atsA).

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Alk_phosphatase (CL0088), which has the following description:

The members of this clan all share a common structure of their catalytic domains, which contain conserved metal binding residues [1].

The clan contains the following 9 members:

Alk_phosphatase DUF1501 DUF229 Metalloenzyme PglZ Phosphodiest Phosphoesterase Sulfatase Sulfatase_C

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(59)
Full
(18763)
Representative proteomes NCBI
(15548)
Meta
(10237)
RP15
(1780)
RP35
(2902)
RP55
(3885)
RP75
(4719)
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Format an alignment

  Seed
(59)
Full
(18763)
Representative proteomes NCBI
(15548)
Meta
(10237)
RP15
(1780)
RP35
(2902)
RP55
(3885)
RP75
(4719)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(59)
Full
(18763)
Representative proteomes NCBI
(15548)
Meta
(10237)
RP15
(1780)
RP35
(2902)
RP55
(3885)
RP75
(4719)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_784 (release 3.0) & Pfam-B_7393 (Release 8.0)
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 59
Number in full: 18763
Average length of the domain: 301.40 aa
Average identity of full alignment: 17 %
Average coverage of the sequence by the domain: 53.82 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 25.0
Noise cut-off 24.9 24.9
Model length: 308
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

Sulfatase

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Sulfatase domain has been found. There are 26 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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