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Information on EC 2.7.1.25 - adenylyl-sulfate kinase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WNM5

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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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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WNM5
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
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, mxan3487, adenosine 5'-phosphosulfate kinase, adenylylsulfate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
the enzyme activity is about 3fold stimulated in the presence of 2 mM dithiothreitol
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ligands, hanging drop vapor diffusion method, using 0.2 M NH4NO3, 20% (w/v) PEG3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C541A
the mutant shows reduced activity compared to the wild type enzyme
C549A
the mutant shows increased activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poyraz, O.e.; Brunner, K.; Lohkamp, B.; Axelsson, H.; Hammarstroem, L.G.; Schnell, R.; Schneider, G.
Crystal structures of the kinase domain of the sulfate-activating complex in Mycobacterium tuberculosis
PLoS ONE
10
e0121494
2015
Mycobacterium tuberculosis (P9WNM5), Mycobacterium tuberculosis
Manually annotated by BRENDA team