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46  structures 1895  species 5  interactions 2431  sequences 25  architectures

Family: ATP-sulfurylase (PF01747)

Summary: ATP-sulfurylase

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

Sulfate adenylyltransferase Edit Wikipedia article

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

In enzymology, a sulfate adenylyltransferase (EC 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.


ATP sulfurylase is one of the enzymes used in pyrosequencing.


  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: 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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Pfam Clan

This family is a member of clan HUP (CL0039), which has the following description:

The HUP class contains the HIGH-signature proteins, UspA superfamily and the PP-ATPase superfamily [1]. The HIGH superfamily has the HIGH Nucleotidyl transferases and the class I tRNA synthetases both of which have the HIGH and the KMSKS motif [1],[2]. The PP-loop ATPase named after the ATP PyroPhosphatase domain, was initially identified as a conserved amino acid sequence motif in four distinct groups of enzymes that catalyse the hydrolysis of the alpha-beta phosphate bond of ATP, namely GMP synthetases, argininosuccinate synthetases, asparagine synthetases, and ATP sulfurylases [3]. The USPA superfamily contains USPA, ETFP and Photolyases [1]

The clan contains the following 26 members:

Arginosuc_synth Asn_synthase ATP-sulfurylase ATP_bind_3 Citrate_ly_lig CTP_transf_like Diphthami_syn_2 ETF FAD_syn HIGH_NTase1 HIGH_NTase1_ass NAD_synthase Pantoate_ligase PAPS_reduct QueC ThiI tRNA-synt_1 tRNA-synt_1_2 tRNA-synt_1b tRNA-synt_1c tRNA-synt_1d tRNA-synt_1e tRNA-synt_1f tRNA-synt_1g tRNA_Me_trans Usp


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

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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: 194
Number in full: 2431
Average length of the domain: 210.30 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 44.66 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.4 23.4
Trusted cut-off 23.4 24.1
Noise cut-off 23.1 23.1
Model length: 212
Family (HMM) version: 13
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Species distribution

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There are 5 interactions for this family. More...

APS_kinase APS_kinase PUA_2 PUA_2 ATP-sulfurylase


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 46 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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