| 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; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| 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 |
| 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 |
| Title | Authors | Date | PubMed 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 RA | 2010 Mar | 20023146 |
| Crystal structure of monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8. | Omi R, Goto M, Miyahara I, Manzoku M, Ebihara A, Hirotsu K | 2007 Nov 6 | 17929834 |
| Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway. | Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M | 2006 Dec 8 | 16966333 |