MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Allochromatium vinosum:
Arabidopsis thaliana col:
Archaeoglobus fulgidus: sulfate adenylyltransferaseInferred from experiment: sat
Desulfocapsa sulfexigens: sulfate adenylyltransferaseInferred from experiment
Desulfovibrio gigas: sulfate adenylyltransferaseInferred from experiment
Desulfovibrio sulfodismutans: sulfate adenylyltransferaseInferred from experiment
endosymbiont of Riftia pachyptila: dissimilatory sulfate adenylyltransferaseInferred from experiment: sat
Escherichia coli K-12 substr. MG1655: sulfate adenylyltransferaseInferred from experiment: cysD, cysN
Homo sapiens:
Saccharomyces cerevisiae: sulfate adenylyltransferaseInferred from experiment: met3
Sinorhizobium meliloti: sulfate adenylyltransferaseInferred from experiment: cysD, cysN

In Pathway: sulfite oxidation III, sulfate activation for sulfonation, sulfate reduction II (assimilatory), sulfate reduction III (assimilatory), sulfate reduction IV (dissimilatory), sulfate reduction V (dissimilatory)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: sulfate adenylyltransferase

Enzyme Commission Synonyms: adenosine-5'-triphosphate sulfurylase, adenosinetriphosphate sulfurylase, adenylylsulfate pyrophosphorylase, ATP sulfurylase, ATP-sulfurylase, sulfurylase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -20.452515Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5′-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC and adenylyl-sulfate kinase ( EC

Citations: [Hilz55, Venkatachalam98]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R00529, Rhea:18133

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O23324, UniProt:RELATED-TO:O33581, UniProt:RELATED-TO:O34764, UniProt:RELATED-TO:O43252, UniProt:RELATED-TO:O48888, UniProt:RELATED-TO:O67174, UniProt:RELATED-TO:P08536, UniProt:RELATED-TO:P13441, UniProt:RELATED-TO:P13442, UniProt:RELATED-TO:P21156, UniProt:RELATED-TO:P23845, UniProt:RELATED-TO:P28604, UniProt:RELATED-TO:P74241, UniProt:RELATED-TO:Q9JUD6, UniProt:RELATED-TO:Q9JUD7, UniProt:RELATED-TO:Q9PM66, UniProt:RELATED-TO:Q10600, UniProt:RELATED-TO:Q12555, UniProt:RELATED-TO:Q12650, UniProt:RELATED-TO:Q27128, UniProt:RELATED-TO:Q39595, UniProt:RELATED-TO:Q43170, UniProt:RELATED-TO:Q43183, UniProt:RELATED-TO:Q43870, UniProt:RELATED-TO:Q96349, UniProt:RELATED-TO:Q96541, UniProt:RELATED-TO:Q9S7D8


Hilz55: Hilz H, Lipmann F (1955). "THE ENZYMATIC ACTIVATION OF SULFATE." Proc Natl Acad Sci U S A 41(11);880-90. PMID: 16589765

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Venkatachalam98: 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. PMID: 9668121

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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