Get   for     ? 
 Site search     ? 
Catalytic Site Atlas Version 2.2.12
Find Annotated Site: PDB code:
Swiss-Prot code:
EC number:
Help
CSA entry for 1j70
Original Entry
Title:
Transferase
Compound:
Atp sulphurylase
Mutant:
No
UniProt/Swiss-Prot:
P08536-MET3_YEAST
EC Class:
2.7.7.4
Other CSA Entries:
Overview of all sites for 1j70
Homologues of 1j70
Entries for UniProt/Swiss-Prot: P08536
Entries for EC: 2.7.7.4
Other Databases:
PDB entry: 1j70
PDBsum entry: 1j70
UniProt/Swiss-Prot: P08536
IntEnz entry: 2.7.7.4
Literature Report:
Introduction:
ATP sulphurylases catalyse the reaction of inorganic sulfate with ATP to form adenosine-5'-phosphosulfate and pyrophosphate in the primary step of intracellular sulfate activation.

ATP sulphurylase is classified into the superfamily of alpha/beta phosphodiesterases.
Mechanism:
ATP sulphurylase catalyses the reaction mostly by simply bringing the substrate in a close proximity and appropriate conformation. ATP is able to make an in-line nucleophilic attack on the adjacent sulfate with stereochemical inversion at the alpha-phosphorous leading directly to the formation of APS with pyrophosphate as a leaving group. The enzyme is able to donate a proton through Arg 197 to facilitate cleavage. The pentavalent transition state is stabilised using His 201 and His 204 side-chains.
Sites:

Click to Display Catalytic Site (Get help with this section)
Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ARGA 197 197Sidechain
Acid/baseSubstrate
Acts as a proton donor to facilitate collapse of the intermediate.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10506138 Related protein: UniProt Q9QYS0 Mutagenesis of residue
PubMed ID 11724564 Related protein: UniProt Q54506 Residue is positioned appropriately (ligand position hypothetical)
PubMed ID 11724564 Related protein: UniProt Q54506 Conservation of residue
PubMed ID 10506138 Related protein: UniProt Q9QYS0 Chemical modification of residue
PubMed ID 107174 Related protein: UniProt Q12650 Chemical modification of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 201 201Sidechain
ElectrostaticTransition state
Stabilises the pentacoordinate transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 9915785 Related protein: UniProt Q43252 Mutagenesis of residue
PubMed ID 11157739 Current protein Conservation of residue
PubMed ID 14983089 Related protein: UniProt Q12650 Residue is positioned appropriately (ligand position known)
PubMed ID 107174 Related protein: UniProt Q12650 Chemical modification of residue
PubMed ID 11724564 Related protein: UniProt Q54506 Conservation of residue
PubMed ID 107174 Related protein: UniProt Q12650 pH dependence of reaction
PubMed ID 14983089 Related protein: UniProt Q12650 Conservation of residue
PubMed ID 11157739 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 10506138 Related protein: UniProt Q9QYS0 Chemical modification of residue
PubMed ID 11724564 Related protein: UniProt Q54506 Residue is positioned appropriately (ligand position hypothetical)
PubMed ID 10506138 Related protein: UniProt Q9QYS0 Mutagenesis of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 204 204Sidechain
ElectrostaticTransition state
Stabilises the pentacoordinate transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 107174 Related protein: UniProt Q12650 pH dependence of reaction
PubMed ID 11724564 Related protein: UniProt Q54506 Conservation of residue
PubMed ID 11724564 Related protein: UniProt Q54506 Residue is positioned appropriately (ligand position hypothetical)
PubMed ID 10506138 Related protein: UniProt Q9QYS0 Mutagenesis of residue
PubMed ID 107174 Related protein: UniProt Q12650 Chemical modification of residue
PubMed ID 14983089 Related protein: UniProt Q12650 Residue is positioned appropriately (ligand position known)
PubMed ID 11157739 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 9915785 Related protein: UniProt Q43252 Mutagenesis of residue
PubMed ID 11157739 Current protein Conservation of residue
PubMed ID 14983089 Related protein: UniProt Q12650 Conservation of residue
PubMed ID 10506138 Related protein: UniProt Q9QYS0 Chemical modification of residue
References:
1
Crystal structure of ATP sulfurylase from the bacterial symbiont of the hydrothermal vent tubeworm Riftia pachyptila.
J. D. Beynon and I. J. MacRae and S. L. Huston and D. C. Nelson and I. H. Segel and A. J. Fisher
Biochemistry 40, (48) 14509-17, (2001).
11724564
2
Adenosine triphosphate sulfurylase from Penicillium chrysogenum. Evidence for essential arginine, histidine, and tyrosine residues.
J. R. Farley and E. A. Christie and P. A. Seubert and I. H. Segel
J Biol Chem 254, (9) 3537-42, (1979).
107174
3
Chemical modification and site-directed mutagenesis of conserved HXXH and PP-loop motif arginines and histidines in the murine bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase.
A. T. Deyrup and B. Singh and S. Krishnan and S. Lyle and N. B. Schwartz
J Biol Chem 274, (41) 28929-36, (1999).
10506138
4
Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation.
T. C. Ullrich and M. Blaesse and R. Huber
EMBO J 20, (3) 316-29, (2001).
11157739
5
Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity.
D. J. Lalor and T. Schnyder and V. Saridakis and D. E. Pilloff and A. Dong and H. Tang and T. S. Leyh and E. F. Pai
Protein Eng 16, (12) 1071-9, (2003).
14983089
6
Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase.
K. V. Venkatachalam and H. Fuda and E. V. Koonin and C. A. Strott
J Biol Chem 274, (5) 2601-4, (1999).
9915785
Which EBI biological databases are available and how do I access them? EBI Site Map