Summary: Sulfatase

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Wikipedia: Sulfatase
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Sulfatase

Steryl-sulfatase

Identifiers

Symbol

Sulfatase

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

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.

[edit] Occurrence and importance

Sulfatases are found in lower and higher organisms. In higher organisms they are found in intracellular and extracellular spaces. 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.

[edit] Three-dimensional structure

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

cerebroside-sulfatase
steryl-sulfatase
arylsulfatase A EC 3.1.6.8 (ASA), a lysosomal enzyme which hydrolyzes cerebroside sulfate;
arylsulfatase B EC 3.1.6.12 (ASB) which hydrolyzes the sulfate ester group from N-acetylgalactosamine 4-sulfate residues of dermatan sulfate;
arylsulfatase C (ASD) and E (ASE); steryl-sulfatase EC 3.1.6.2 (STS), a membrane bound enzyme which hydrolyzes 3-beta-hydroxy steroid sulfates;
iduronate 2-sulfatase EC 3.1.6.13 (IDS), a lysosomal enzyme that hydrolyzes the 2-sulfate groups from iduronic acids in dermatan sulfate and heparan sulfate;
N-acetylgalactosamine-6-sulfatase EC 3.1.6.4, which hydrolyzes the 6-sulfate groups of the N-acetyl-D-galactosamine of chondroitin sulfate and D-galactose 6-sulfate units of keratan sulfate;
N-sulfoglucosamine sulfohydrolase EC 3.10.1.1, the lysosomal enzyme that hydrolyses N-sulfo-D-glucosamine into glucosamine and sulfate;
glucosamine-6-sulfatase EC 3.1.6.14 (G6S), which hydrolyzes the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate;
N-sulfoglucosamine sulfohydrolase EC 3.10.1.1, the lysosomal enzyme that hydrolyses N-sulfo-D-glucosamine into glucosamine and sulfate;
sea urchin embryo arylsulfatase EC 3.1.6.1;
green algae arylsulfatase EC 3.1.6.1, which plays a role in the mineralization^{[disambiguation needed ]} of sulfates; and
arylsulfatase EC 3.1.6.1 from Escherichia coli, Klebsiella aerogenes and Pseudomonas aeruginosa.

[edit] Human proteins containing this domain

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

[edit] References

^ 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.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=54990.
^ 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.

[edit] External links

This enzyme-related article is a stub. You can help Wikipedia by expanding it.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic ester hydrolases

Cholinesterase (Acetylcholinesterase, Butyrylcholinesterase) · Pectinesterase · 6-phosphogluconolactonase · PAF acetylhydrolase

Lipase (Bile salt-dependent, Gastric/Lingual, Pancreatic, Lysosomal, Hormone-sensitive, Endothelial, Hepatic, Lipoprotein, Monoacylglycerol, Diacylglycerol)

Phospholipase (A1, A2, B)

3.1.2: Thioesterase

Palmitoyl protein thioesterase · Ubiquitin carboxy-terminal hydrolase L1

3.1.3: Phosphatase

Alkaline phosphatase (ALPI, ALPL, ALPP) · Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases · Nucleotidase · Glucose 6-phosphatase · Fructose 1,6-bisphosphatase · Calcineurin · Phosphoprotein phosphatase (PP2A) · OCRL · Pyruvate dehydrogenase phosphatase · Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase · PTEN · Phytase · Inositol-phosphate phosphatase (IMPA1)

Phosphoprotein phosphatase: Protein tyrosine phosphatase · Protein serine/threonine phosphatase · Dual-specificity phosphatase

3.1.4: Phosphodiesterase

Autotaxin · Phospholipase (C, D) · Sphingomyelin phosphodiesterase (1) · PDE1 · PDE2 · PDE3 · PDE4A/PDE4B · PDE5 · Lecithinase (Clostridium perfringens alpha toxin) · Cyclic nucleotide phosphodiesterase

3.1.6: Sulfatase

arylsulfatase (Arylsulfatase A, Arylsulfatase B, Arylsulfatase E, Steroid sulfatase) · Galactosamine-6 sulfatase · Iduronate-2-sulfatase · N-acetylglucosamine-6-sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I · Deoxyribonuclease II · Deoxyribonuclease IV · Restriction enzyme · UvrABC endonuclease

Endoribonuclease	RNase III · RNase H (1, 2A, 2B, 2C) · RNase P · RNase A (1, 2, 3, 4/5) · RNase T1 · RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 · Micrococcal nuclease

B
enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
2.7.10
2.7.11-12
3.1
- 2
- 3
- 4
- 5
- 6
- 7
3.1.3.48
3.4.21
- 22
- 23
- 24
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

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.

Sulfatase

No Pfam abstract.

Literature references

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

Clan

This family is a member of clan Alk_phosphatase (CL0088), which has a total of 8 members.

Internal database links

Similarity to PfamA using HHSearch:

DUF229 Phosphodiest Metalloenzyme DUF3260

External database links

HOMSTRAD:	Sulfatase
PANDIT:	PF00884
PROSITE:	PDOC00117
Pseudofam:	PF00884
SCOP:	1auk
SYSTERS:	Sulfatase

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], including 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.

Molecular function	sulfuric ester hydrolase activity (GO:0008484)
Biological process	metabolic process (GO:0008152)

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 contains the following 8 members:

Alk_phosphatase DUF1501 DUF229 Metalloenzyme PglZ Phosphodiest Phosphoesterase Sulfatase

Alignments

There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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Alignment:	Seed (59) Full (12569) NCBI (12878) Metagenomics (11172)
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Alignment:	Seed (59) Full (12569)
Format:
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Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.

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

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:	Seed (59) Full (12569) NCBI (12878) Metagenomics (11172)
Full length sequences	Full-sequences (12569)

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. 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 or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

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

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:

12569

Average length of the domain:

370.60 aa

Average identity of full alignment:

15 %

Average coverage of the sequence by the domain:

65.30 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	20.0	20.0
Trusted cut-off	20.0	20.0
Noise cut-off	19.9	19.9

Model length:

379

Family (HMM) version:

18

Download:

download the raw HMM for this family

Species distribution

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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab if you need to select sub-trees and view sequence alignments. More...

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How the sunburst is generated

The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, it's distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.

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Unmapped species names

The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

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Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

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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 13 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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Family: Sulfatase (PF00884)

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Summary: Sulfatase

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Sulfatase

Contents

[edit] Occurrence and importance

[edit] Three-dimensional structure

[edit] Human proteins containing this domain

[edit] References

[edit] External links

Sulfatase

Literature references

Clan

Internal database links

External database links

InterPro entry IPR000917

Gene Ontology

Domain organisation

Pfam Clan

Alignments

Viewing

Downloading

View options

Formatting options

Download options

External links

HMM logo

Trees

Curation and family details

Curation

HMM information

Species distribution

Sunburst controls

Weight segments by...

Change the size of the sunburst

Colour assignments

How the sunburst is generated

Colouring and labels

Anomalies in the taxonomy tree

Missing taxonomic levels

Unmapped species names

Sub-species

Too many species/sequences

Tree controls

Annotation

Download tree

Selected sequences

Species trees

Interactive tree

Interactions

Structures