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CSA entry for 1d2t
Original Entry
Title:
Hydrolase
Compound:
Acid phosphatase
Mutant:
No
UniProt/Swiss-Prot:
Q9S1A6-Q9S1A6
EC Class:
3.1.3.2
Other CSA Entries:
Overview of all sites for 1d2t
Homologues of 1d2t
Entries for UniProt/Swiss-Prot: Q9S1A6
Entries for EC: 3.1.3.2
Other Databases:
PDB entry: 1d2t
PDBsum entry: 1d2t
UniProt/Swiss-Prot: Q9S1A6
IntEnz entry: 3.1.3.2
Literature Report:
Introduction:
Non-specific acid phosphatases (NSAPs) catalyse the hydrolysis of phosphate monoesters. They may be divided into three classes (A, B, C) based on sequence similarity.The Escherichia blattae enzyme (EB-NSAP) is a class A NSAP. It is a histidine phosphatase, catalysing hydrolysis via a phophohistidine intermediate. This enzyme will dephosphorylate a range of phosphoesters, including p-nitrophenyl phosphate, carbamoyl phosphate, pyrophosphate, glucose-6-phosphate, and ATP. As with some other NSAPs, it will also catalyse phosphotransfer reactions such as the transfer of phosphate from pyrophosphate to glucose.
Mechanism:
The reaction proceeds via a phosphoenzyme intermediate. His 189 functions as a nucleophile to attack the phosphate group, while the departing alcohol is protonated by His 150. Asp 193 functions to modify the nucleophilic properties of His 189, while Arg 183 is proposed to help stabilise the resulting phosphohistidine intermediate. In the second step, the phosphohistidine intermediate is hydrolysed by a water molecule that is deprotonated by His 150.
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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 150 168Sidechain
Acid/baseSubstrate
Acid/baseWater
Protonates the departing alcohol on attack by His 189. Deprotonates the water molecule that hydrolyses the phosphoenzyme intermediate.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10835340 Current protein Structural similarity to homologue of known mechanism
PubMed ID 10835340 Current protein Conservation of residue
PubMed ID 10835340 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ARGA 183 201Sidechain
ElectrostaticTransition state
Proposed to stabilise the phosphoenzyme intermediate.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10835340 Current protein Conservation of residue
PubMed ID 10835340 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 189 207Sidechain
NucleophileSubstrate
Attacks the phosphate group of the substrate, leading to formation of a covalent phosphoenzyme intermediate.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10835340 Current protein Chemical modification of residue
PubMed ID 10835340 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 10835340 Current protein Residue is covalently bound to intermediate, based on structural data
PubMed ID 10835340 Current protein Structural similarity to homologue of known mechanism
PubMed ID 10835340 Current protein Conservation of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPA 193 211Sidechain
ElectrostaticResidue
Modifies the nucleophilic properties of His 189.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10835340 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 10835340 Current protein Structural similarity to homologue of known mechanism
References:
1
X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.
K. Ishikawa and Y. Mihara and K. Gondoh and E. Suzuki and Y. Asano
EMBO J 19, (11) 2412-23, (2000).
10835340
2
An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
A. F. Neuwald
Protein Sci 6, (8) 1764-7, (1997).
9260289
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