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Information on EC 2.7.1.25 - adenylyl-sulfate kinase and Organism(s) Thiobacillus denitrificans and UniProt Accession Q3SM86

for references in articles please use BRENDA:EC2.7.1.25
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IUBMB Comments
The human phosphoadenosine-phosphosulfate synthase (PAPSS) 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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
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Thiobacillus denitrificans
UNIPROT: Q3SM86
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The taxonomic range for the selected organisms is: Thiobacillus denitrificans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aps kinase, papss1, aps-kinase, paps synthetase, papss, paps synthase, adenosine-5'-phosphosulfate kinase, adenosine 5'-phosphosulfate kinase, mxan3487, adenylylsulfate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgATP:APS 3'-phosphotransferase
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3'-phosphoadenosine-5'-phosphosulfate synthetase
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5'-phosphoadenosine sulfate kinase
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adenosine 5'-phosphosulfate kinase
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adenosine phosphosulfate kinase
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adenosine phosphosulfokinase
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adenosine-5'-phosphosulfate 3'-phosphotransferase
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adenosine-5'-phosphosulfate-3'-phosphokinase
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adenosine-5'phosphosulfate kinase
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adenylylsulfate 3'-phosphotransferase
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adenylylsulfate kinase
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APS kinase
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ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
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kinase, adenylylsulfate (phosphorylating)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:adenylyl-sulfate 3'-phosphotransferase
The human phosphoadenosine-phosphosulfate synthase (PAPSS) 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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
CAS REGISTRY NUMBER
COMMENTARY hide
9012-38-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
MgATP2- + adenosine 5'-phosphosulfate
MgADP- + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60500
6 * 60500, calculated, crystall structure analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
6 * 60500, calculated, crystall structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gay, S.C.; Segel, I.H.; Fisher, A.J.
Structure of the two-domain hexameric APS kinase from Thiobacillus denitrificans: structural basis for the absence of ATP sulfurylase activity
Acta Crystallogr. Sect. D
65
1021-1031
2009
Thiobacillus denitrificans (Q3SM86), Thiobacillus denitrificans
Manually annotated by BRENDA team