Enzyme

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EC Tree
     3. Hydrolases
        3.9 Acting on phosphorus-nitrogen bonds
            3.9.1 Acting on phosphorus-nitrogen bonds (only sub-subclass identified to date)
ID:3.9.1.2
Description:Protein arginine phosphatase.
Cath: 3.40.50.2300;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.9.1.2
BRENDA Enzyme Link: BRENDA 3.9.1.2
KEGG Enzyme Link: KEGG3.9.1.2
BioCyc Enzyme Link: BioCyc 3.9.1.2
ExPASy Enzyme Link: ExPASy3.9.1.2
EC2PDB Enzyme Link: EC2PDB 3.9.1.2
ExplorEnz Enzyme Link: ExplorEnz 3.9.1.2
PRIAM enzyme-specific profiles Link: PRIAM 3.9.1.2
IntEnz Enzyme Link: IntEnz 3.9.1.2
MEDLINE Enzyme Link: MEDLINE 3.9.1.2
MSA:

3.9.1.2;

Phylogenetic Tree:

3.9.1.2;

Uniprot:
M-CSA:
RHEA:43380 H2O + N(omega)-phospho-L-arginyl-[protein] = L-arginyl-[protein] + phosphate
RULE(radius=1) [*:1]-[NH;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[NH2;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Chasing Phosphoarginine Proteins: Development of a Selective Enrichment Method Using a Phosphatase Trap.Trentini DB, Fuhrmann J, Mechtler K, Clausen T2014 Aug24825175
Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria.Fuhrmann J, Mierzwa B, Trentini DB, Spiess S, Lehner A, Charpentier E, Clausen T2013 Jun 2723770242