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36  structures 1032  species 2  interactions 1308  sequences 15  architectures

Family: ATP-sulfurylase (PF01747)

Summary: ATP-sulfurylase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Sulfate adenylyltransferase". More...

Sulfate adenylyltransferase Edit Wikipedia article

sulfate adenylyltransferase (ATP)
Identifiers
EC number 2.7.7.4
CAS number 9012-39-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
ATP-sulfurylase
PDB 1v47 EBI.jpg
crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps
Identifiers
Symbol ATP-sulfurylase
Pfam PF01747
InterPro IPR002650
SCOP 1i2d
SUPERFAMILY 1i2d

In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction

ATP + sulfate \rightleftharpoons diphosphate + adenylyl sulfate

Thus, the two substrates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:sulfate adenylyltransferase. Other names in common use include adenosine-5'-triphosphate sulfurylase, adenosinetriphosphate sulfurylase, adenylylsulfate pyrophosphorylase, ATP sulfurylase, ATP-sulfurylase, and sulfurylase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.

Some sulfate adenylyltransferases are part of a bifunctional polypeptide chain associated with adenosyl phosphosulfate (APS) kinase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate.[1][2]

Structural studies[edit]

As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes 1G8F, 1G8G, 1G8H, 1I2D, 1J70, 1JEC, 1JED, 1JEE, 1JHD, 1M8P, 1R6X, 1TV6, 1V47, 1X6V, 1XJQ, 1XNJ, 1ZUN, and 2GKS.

Applications[edit]

ATP sulfurylase is one of the enzymes used in pyrosequencing.

References[edit]

  1. ^ Rosenthal E, Leustek T (November 1995). "A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities". Gene 165 (2): 243–8. doi:10.1016/0378-1119(95)00450-K. PMID 8522184. 
  2. ^ Kurima K, Warman ML, Krishnan S, Domowicz M, Krueger RC, Deyrup A, Schwartz NB (July 1998). "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8681–5. doi:10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738. 

Further reading[edit]

  • Bandurski RS, Wilson LG, Squires CL (1956). "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78 (24): 6408–6409. doi:10.1021/ja01605a028. 
  • Hilz H and Lipmann F (1955). "The enzymatic activation of sulfate". Proc. Natl. Acad. Sci. USA 41 (11): 880–890. doi:10.1073/pnas.41.11.880. 
  • Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. doi:10.1074/jbc.273.30.19311. PMID 9668121. 

This article incorporates text from the public domain Pfam and InterPro IPR002650

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.

ATP-sulfurylase Provide feedback

This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase PF01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate [2]. ATP sulfurylase catalyses the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate [1].

Literature references

  1. Kurima K, Warman ML, Krishnan S, Domowicz M, Krueger RC Jr, Deyrup A, Schwartz NB; , Proc Natl Acad Sci U S A 1998;95:8681-8685.: A member of a family of sulfate-activating enzymes causes murine brachymorphism [published erratum appears in Proc Natl Acad Sci U S A 1998 Sep 29;95(20):12071] PUBMED:9671738 EPMC:9671738

  2. Rosenthal E, Leustek T; , Gene 1995;165:243-248.: A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities. PUBMED:8522184 EPMC:8522184


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR024951

This domain is the catalytic domain of ATP-sulfurylase or sulphate adenylyltransferase (EC). ATP-sulfurylase catalyses the synthesis of adenosine-phosphosulphate (APS) from ATP and inorganic sulphate [PUBMED:9671738]. Sometimes is found as part of a bifunctional polypeptide chain associated with adenylylsulphate kinase (INTERPRO). Both enzymes are required for PAPS (phosphoadenosine-phosphosulphate) synthesis from inorganic sulphate [PUBMED:8522184].

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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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
(113)
Full
(1308)
Representative proteomes NCBI
(1170)
Meta
(549)
RP15
(179)
RP35
(315)
RP55
(435)
RP75
(520)
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Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(113)
Full
(1308)
Representative proteomes NCBI
(1170)
Meta
(549)
RP15
(179)
RP35
(315)
RP55
(435)
RP75
(520)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(113)
Full
(1308)
Representative proteomes NCBI
(1170)
Meta
(549)
RP15
(179)
RP35
(315)
RP55
(435)
RP75
(520)
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.

Pfam alignments:

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_494 (release 4.2)
Previous IDs: none
Type: Domain
Author: Bashton M, Bateman A
Number in seed: 113
Number in full: 1308
Average length of the domain: 214.80 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 43.51 %

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 23.4 23.4
Trusted cut-off 24.4 23.9
Noise cut-off 22.8 22.8
Model length: 215
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

APS_kinase ATP-sulfurylase

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 ATP-sulfurylase domain has been found. There are 36 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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