Information on EC 2.7.7.4 - sulfate adenylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.7.7.4
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RECOMMENDED NAME
GeneOntology No.
sulfate adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Metabolic pathways
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Microbial metabolism in diverse environments
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Monobactam biosynthesis
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Purine metabolism
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selenate reduction
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Selenocompound metabolism
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sulfate activation for sulfonation
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sulfate reduction II (assimilatory)
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sulfate reduction III (assimilatory)
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sulfate reduction IV (dissimilatory, to hydrogen sufide))
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sulfate reduction V (dissimilatory, to thiosulfate)
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sulfite oxidation III
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Sulfur metabolism
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sulfate reduction
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SYSTEMATIC NAME
IUBMB Comments
ATP:sulfate adenylyltransferase
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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
CAS REGISTRY NUMBER
COMMENTARY hide
9012-39-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene sat
UniProt
Manually annotated by BRENDA team
gene sat
UniProt
Manually annotated by BRENDA team
Columbi aecotype
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Brassica capitata
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain Cm
SwissProt
Manually annotated by BRENDA team
strain Cm
SwissProt
Manually annotated by BRENDA team
isolated from the human large intestine
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Manually annotated by BRENDA team
isolated from the human large intestine
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Manually annotated by BRENDA team
isolated from the human large intestine
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Manually annotated by BRENDA team
isolated from the human large intestine
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Manually annotated by BRENDA team
mixed SRB (sulfate reducing bacteria)-containing consortium consisting mainly of the Desulfovibrio genus
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Manually annotated by BRENDA team
Klebs var. bacillaris Cori, aplastidic mutant W10BSmL
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Manually annotated by BRENDA team
strain NCA 1503
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Manually annotated by BRENDA team
strain NCA 1503
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Penicillium duponti
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Sacardo, strongly sulfite producing strain
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Manually annotated by BRENDA team
Sacardo, strongly sulfite producing strain
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
isozymes APS1, APS2, and APS4
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Manually annotated by BRENDA team
6301
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Manually annotated by BRENDA team
6301
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Manually annotated by BRENDA team
gene sat
UniProt
Manually annotated by BRENDA team
gene sat
UniProt
Manually annotated by BRENDA team
gene THAPSDRAFT_269714
UniProt
Manually annotated by BRENDA team
gene THAPSDRAFT_269714
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + CrO42-
AMP + adenylyl-chromate
show the reaction diagram
ATP + FPO32-
?
show the reaction diagram
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-
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
ATP + SeO42-
AMP + adenylylselenate
show the reaction diagram
ATP + sulfate
adenylyl sulfate + diphosphate
show the reaction diagram
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-
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-
?
ATP + sulfate
ADP + adenylyl sulfate
show the reaction diagram
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
ATP + WO42-
AMP + adenylyl-wolframate
show the reaction diagram
dATP + SO42-
diphosphate + deoxyadenylylsulfate
show the reaction diagram
diphosphate + adenylyl sulfate
ATP + sulfate
show the reaction diagram
MgATP2- + adenylyl sulfate
MgADP- + 3-phosphoadenylyl sulfate
show the reaction diagram
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reaction carried out by the APS kinase activity of the bifunctional enzyme
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r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
show the reaction diagram
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reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
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r
MgATP2- + sulfate
Mg-diphosphate + adenylyl sulfate
show the reaction diagram
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r
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
ADP + adenylyl sulfate
show the reaction diagram
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
diphosphate + adenylyl sulfate
ATP + sulfate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
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stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Cobalt
Fe2+
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stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
SO42-
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stimulatory to ATPS
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-adenosine diphosphate
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3'-phosphoadenosine 5'-phosphosulfate
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allosteric, binding of the inhibitor to the catalytic site as well as to the allosteric site of the wild type enzyme acts to decrease the degree of cooperativity
3'-phosphoadenosine-5'-phosphate
3'-phosphoadenosine-5'-phosphosulfate
5,5'-dithiobis(2-nitrobenzoic acid)
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0.05 mM, rapid decrease in activity of wild-type enzyme (t1/2: 20 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min
adenosine 5'-monosulfate
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adenosine 5'-phosphoramidate
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adenosine 5'-phosphosulfate
adenylyl sulfate
APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site; APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site
Ba2+
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2 mM
beta-fluoro-adenosine 5'-phosphosulfate
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beta-methylene-adenosine 5'-phosphosulfate
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ClO3-
deoxyadenylylsulfate
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1 mM, in presence of about 20% inhibition
diacetyl
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significant inhibition in the presence of borate, protection by adenosine 5'-phosphosulfate, ATP or MgATP2- plus nitrate
diphosphate
FSO3-
guanylylsulfate
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1 mM, in presence of adenylylsulfate about 20% inhibition
inosylylsulfate
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1 mM, in presence of adenylylsulfate about 20% inhibition
iodoacetic acid
methylene blue
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inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate
MgATP2-
molybdate
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N-Acetylimidazole
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76% of the original activity can be restored by treatment with hydroxylamine
N-ethylmaleimide
Ni2+
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2 mM
PCMB
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5 mM, inhibits reaction with diphosphate and adenylylsulfate
Phenylglyoxal
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3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
phosphate
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inhibition is enhanced by increasing concentrations of Mg2+
S2O32-
SeO42-
SO32-
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1 mM, 10-25% inhibition
SO42-
Sulfide
Tetranitromethane
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partial
thiosulfate
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competitive with molybdate and noncompetitive with MgATP
Tris-malic acid-KOH buffer
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Zn2+
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inhibitory effect even at concentrations as low as 40 mg/l
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine-5'-phosphosulfate reductase 1
slight stimulation of ATPS1 activity is noted with the addition of the 5fold volume of full-length adenosine-5'-phosphosulfate reductase 1
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AMP
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activates
dithiothreitol
activates
FSO3-
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activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
S2O32-
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activates SO42dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.17
adenosine 5'-phosphosulfate
0.0044 - 2.95
adenylyl sulfate
0.0004 - 0.025
adenylylsulfate
0.027 - 2.6
ATP
0.12
CrO42-
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30C, pH 8.0
0.16 - 0.84
dATP
0.00071 - 19.41
diphosphate
1.3
FPO32-
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pH 8.0, 30C, chloroplastic enzyme
0.0191
magnesium diphosphate
reverse reaction, ATP synthesis
0.0077 - 1.1
MgATP2-
1.3
molybdate
pH 8.0, 30C
0.076 - 0.64
MoO42-
0.1 - 1
SeO42-
0.18 - 3.3
SO42-
0.00211 - 17
sulfate
0.47
WO42-
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30C, pH 8.0
additional information
additional information
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