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Information on EC 2.7.7.4 - sulfate adenylyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LIK9
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2.7.7.4 sulfate adenylyltransferaseIUBMB Comments
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).
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- 2.7.7.4
-
two-phase
- peg
- glycol
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bottom
- dextran
-
peg-rich
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liquid-liquid
-
biomolecules
-
assimilatory
- vr
- chrysogenum
- k2hpo4
-
diagram
-
sulfotransferase
- selenate
-
microfluidic
- sulfite
-
counter-current
-
e-cigarettes
- juncea
- o-acetylserine
- na2so4
- phytochelatins
-
ultrasonic-assisted
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screw
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immiscible
-
sults
- chlorate
-
cigar
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
atps, atp sulfurylase, papss2, atp-sulfurylase, sulfurylase, atp sulphurylase, sulfate adenylyltransferase, atps2, atps1, atp-s, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphate sulphurylase
-
-
-
-
adenosine 5'-triphosphate-sulfurylase
-
-
-
-
adenosine triphosphate sulphurylase
-
-
-
-
adenosine-5'-triphosphate sulfurylase
-
-
-
-
adenosinetriphosphate sulfurylase
-
-
-
-
adenylylsulfate pyrophosphorylase
-
-
-
-
adenylyltransferase, sulfate
-
-
-
-
ATP sulfurylase
ATP-sulfurylase
sulfurylase
-
-
-
-
ATP sulfurylase
-
-
-
-
ATP-sulfurylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
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
9012-39-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.135
0.14
0.145
recombinant wild-type enzyme ATPS1 and mutant A337S, pH 8.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Arabidopsis thaliana has isozymes with N-terminal extensions typical of plastid-transit-peptides
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
isozyme ATPS2 is dually encoded in plastidic and cytosolic forms, where translational initiation at AUGMet1 and AUGMet52 or AUGMet58 produce ATPS2 in plastid and cytosol, respectively
isozyme ATPS2 is dually encoded in plastidic and cytosolic forms, where translational initiation at AUGMet1 and AUGMet52 or AUGMet58 produce ATPS2 in plastid and cytosol, respectively
additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
-
additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
-
additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
-
additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
-
additional information
isozyme ATPS2 is alternatively translated into two different isoforms that dually localize in plastids and cytosol in Arabidopsis thaliana. Molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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additional information
-
isozyme ATPS2 is alternatively translated into two different isoforms that dually localize in plastids and cytosol in Arabidopsis thaliana. Molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
plants with the Bay allele of ATPS1 accumulate lower steady-state levels of ATPS1 transcript than those with the Sha allele, which leads to lower enzyme activity and, ultimately, the accumulation of sulfate. Examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher. The contents of glutathione are not affected by the disruption of ATPS1 in Col-0 but are lower in Shahdara and both HIF004 lines compared with Bay-0 and the Col-0 genotypes
metabolism
physiological function
metabolism
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
additional information
sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, overview
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
metabolism
ATP sulfurylase precedes adenosine 5'-phosphosulfate reductase in the sulfate assimilation pathway. The ATPS1 transcript variation is controlled in cis
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
sulfate content in Arabidopsis thaliana is controlled by two genes encoding subsequent enzymes in the sulfate assimilation pathway but using different mechanisms, variation in amino acid sequence and variation in expression levels
physiological function
upon expression in Medicago sativa, transgenic plants grow more efficiently compared with their non-transgenic counterparts under heavy metal stress conditions, with significant increase in shoot and root dry weight. Transgenic lines show higher levels of heavy metal accumulation in shoot and root tissues. The transgenic lines are fertile and do not exhibit any apparent morphological abnormality
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
metabolism
molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). APS1_ARATH
463
0
51459
Swiss-Prot
Chloroplast (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A337S
site-directed mutagenesis, shows activity unaltered to the wild-type enzyme
E169A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
G342D
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
G56S
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
L122V
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
S9R
site-directed mutagenesis, a transit peptide mutant, inactive mutant
T198A
site-directed mutagenesis, shows activity similar to the wild-type enzyme
V316F
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
V43N
site-directed mutagenesis, a transit peptide mutant, shows activity similar to the wild-type enzyme
M1L/M4L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M52L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M52L/M58
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M58L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M52L/M58L
site-directed mutagenesis, cytosolic localization of the mutant
M4L/M52L/M58L
site-directed mutagenesis, chloroplastidic localization of the mutant
M52L/M58L
site-directed mutagenesis, chloroplastidic localization of the mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene atps1 or At3g22890, examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher
the four ATP-S genes ATPS1,-2,-3, and -4 have N-terminal extensions typ ical of plastid-transit peptides, and are located on different chromosomes
gene APS2 or At1g19920, Arabidopsis thaliana APS isozyme sequence comparisons, protoplast isolation and transfection of APS2, expression of GFP(S65T)-tagged enzyme under control of CaMV 35S promoter, the binary plasmids are transferred to Agrobacteriumtume faciens C58C1 GV3101 that are transformed by floral dip method into plants. Translationof ATPS2 mRNA starts at multiple sites, AUGMet1 and eitherAUGMet52 or AUGMet58, to produce the plastidic and the cytosolic ATPS2 isoforms, respectively, in Arabidopsis thaliana. The alternative translational initiation sites of ATPS2 are determined by expression of dual-luciferase-tagged fusion constructs of wild-type and mutant isozyme ATPS2 in Arabidopsis protoplasts. The translation of chloroplastic ATPS2 pre-protein can only be initiated from the AUGMet1 start codon
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ATP-S activity/expression can also be controlled/modulated by S-limitation1 (SLIM1), a transcription factor identical to ethylene-insensitive3-like (EIL3) transcription factor in Arabidopsis and the regulator of many S-deficiency responsive genes
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion-mediates regulation of ATP-S activity/expression. Expression of both ATPS1 and ATPS3 isoforms is controlled by all six GSs-related MYBTFs, namely MYB28, MYB29, and MYB76, MYB51, MYB34, and MYB122. Isozymes ATPS1 and ATPS3 are strongly associated with the control of synthesis of aliphatic and indolic GSs, respectively. Arabidopsis thaliana overexpressing or disruption in MYB51-gene shows alterations in ATP-S-transcript levels and activity. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
ATP-S activity/expression can also be controlled/modulated by S-limitation1 (SLIM1), a transcription factor identical to ethylene-insensitive3-like (EIL3) transcription factor in Arabidopsis and the regulator of many S-deficiency responsive genes
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthora infestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion mediates regulation of ATP-S activity/expression. ATP-S isoforms can be differentially expressed by S-depletion, e.g. isozyme APS3, while isozyme APS2 is insensitive to S-depletion. Arabidopsis thaliana overexpressing or disruption in MYB51-gene shows alterations in ATP-S-transcript levels and activity. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthora infestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion mediates regulation of ATP-S activity/expression. ATP-S isoforms can be differentially expressed by S-depletion, e.g. isozyme APS3, while isozyme APS2 is insentivie to S depletion. Expression of both ATPS1 and ATPS3 isoforms is controlled by all six GSs-related MYBTFs, namely MYB28, MYB29, and MYB76, MYB51, MYB34, and MYB122. Isozymes ATPS1 and ATPS3 are strongly associated with the control of synthesis of aliphatic and indolic GSs, respectively. Arabidopsis thaliana overexpressing or disruption in MYB51-gene shows alterations in ATP-S-transcript levels and activity. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthora infestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion mediates regulation of ATP-S activity/expression. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bohrer, A.S.; Yoshimoto, N.; Sekiguchi, A.; Rykulski, N.; Saito, K.; Takahashi, H.
Alternative translational initiation of ATP sulfurylase underlying dual localization of sulfate assimilation pathways in plastids and cytosol in Arabidopsis thaliana
Front. Plant Sci.
5
750
2014
Arabidopsis thaliana (Q43870), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q43870)
Anjum, N.A.; Gill, R.; Kaushik, M.; Hasanuzzaman, M.; Pereira, E.; Ahmad, I.; Tuteja, N.; Gill, S.S.
ATP-sulfurylase, sulfur-compounds, and plant stress tolerance
Front. Plant Sci.
6
210
2015
Avena sativa, Brassica juncea, Brassica napus, Hordeum vulgare, Lemna gibba, Lepidium sativum, Nicotiana tabacum, Oryza sativa, Triticum aestivum, Zea mays, Noccaea caerulescens, Sedum alfredii, Stanleya pinnata, Salvinia minima, Glycine max (I1LWX5), Glycine max (I1N6H7), Glycine max (I1NGL3), Glycine max (Q8SAG1), Arabidopsis thaliana (O23324), Arabidopsis thaliana (Q43870), Arabidopsis thaliana (Q9LIK9), Arabidopsis thaliana (Q9S7D8), Camellia sinensis (Q1HL01), Camellia sinensis (Q1HL02)
Herrmann, J.; Ravilious, G.E.; McKinney, S.E.; Westfall, C.S.; Lee, S.G.; Baraniecka, P.; Giovannetti, M.; Kopriva, S.; Krishnan, H.B.; Jez, J.M.
Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation
J. Biol. Chem.
289
10919-10929
2014
Glycine max (Q8SAG1), Glycine max, Arabidopsis thaliana (Q9LIK9), Arabidopsis thaliana Col-0 (Q9LIK9)
Koprivova, A.; Giovannetti, M.; Baraniecka, P.; Lee, B.R.; Grondin, C.; Loudet, O.; Kopriva, S.
Natural variation in the ATPS1 isoform of ATP sulfurylase contributes to the control of sulfate levels in Arabidopsis
Plant Physiol.
163
1133-1141
2013
Arabidopsis thaliana (Q9LIK9), Arabidopsis thaliana Col-0 (Q9LIK9)
Kumar, V.; AlMomin, S.; Al-Shatti, A.; Al-Aqeel, H.; Al-Salameen, F.; Shajan, A.B.; Nair, S.M.
Enhancement of heavy metal tolerance and accumulation efficiency by expressing Arabidopsis ATP sulfurylase gene in alfalfa
Int. J. Phytoremediation
21
1112-1121
2019
Arabidopsis thaliana (Q9LIK9)
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