Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.15
Description:Histidinol-phosphatase.
Cath: 3.20.20.140; 3.40.50.1000;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.15
BRENDA Enzyme Link: BRENDA 3.1.3.15
KEGG Enzyme Link: KEGG3.1.3.15
BioCyc Enzyme Link: BioCyc 3.1.3.15
ExPASy Enzyme Link: ExPASy3.1.3.15
EC2PDB Enzyme Link: EC2PDB 3.1.3.15
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.15
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.15
IntEnz Enzyme Link: IntEnz 3.1.3.15
MEDLINE Enzyme Link: MEDLINE 3.1.3.15
MSA:

3.1.3.15;

Phylogenetic Tree:

3.1.3.15;

Uniprot:
M-CSA:
RHEA:14465 H2O + L-histidinol phosphate = L-histidinol + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.Petersen LN, Marineo S, Mandalà S, Davids F, Sewell BT, Ingle RA2010 Mar20023146
Crystal structure of monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8.Omi R, Goto M, Miyahara I, Manzoku M, Ebihara A, Hirotsu K2007 Nov 617929834
Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway.Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M2006 Dec 816966333