EC number:3.5.4.30
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.4 In cyclic amidines |
| ID: | 3.5.4.30 |
|---|---|
| Description: | dCTP deaminase (dUMP-forming). |
| Cath: | 2.70.40.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.4.30 |
| BRENDA Enzyme Link: | BRENDA 3.5.4.30 |
| KEGG Enzyme Link: | KEGG3.5.4.30 |
| BioCyc Enzyme Link: | BioCyc 3.5.4.30 |
| ExPASy Enzyme Link: | ExPASy3.5.4.30 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.4.30 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.4.30 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.4.30 |
| IntEnz Enzyme Link: | IntEnz 3.5.4.30 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.4.30 |
| RHEA:19205 | dCTP + 2 H2O = diphosphate + dUMP + NH4(+) |
| RULE(radius=1) | ([*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]:[n;H0;+0:8]:[c;H0;+0:9](:[*:10])-[NH2;+0:11]).[OH2;+0:12].[OH2;+0:13]>>([*:1]-[OH;+0:2].[*:7]:[nH;+0:8]:[c;H0;+0:9](:[*:10])=[O;H0;+0:13]).[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:12].[NH3;+0:11] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii. | Huffman JL, Li H, White RH, Tainer JA | 2003 Aug 22 | 12909016 |
| Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases. | Johansson E, Bjornberg O, Nyman PO, Larsen S | 2003 Jul 25 | 12756253 |
| The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. | Li H, Xu H, Graham DE, White RH | 2003 Mar 28 | 12538648 |