| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.15.32 |
|---|---|
| Description: | Pentalenene oxygenase. |
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 1.14.15.32 |
| BRENDA Enzyme Link: | BRENDA 1.14.15.32 |
| KEGG Enzyme Link: | KEGG1.14.15.32 |
| BioCyc Enzyme Link: | BioCyc 1.14.15.32 |
| ExPASy Enzyme Link: | ExPASy1.14.15.32 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.15.32 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.15.32 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.15.32 |
| IntEnz Enzyme Link: | IntEnz 1.14.15.32 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.15.32 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:31699 | 4 H(+) + 2 O2 + pentalenene + 4 reduced [2Fe-2S]-[ferredoxin] = 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin] + pentalen-13-al |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[CH3;+0:10].[*:11]-[N;H0;+0:12]1-[CH;+0:13]=[C;H0;+0:14](-[*:15])-[CH2;+0:16]-[CH;+0:17]=[CH;+0:18]-1.[H+;H0:19].[H+;H0:20].[O;H0;+0:21]=[O;H0;+0:22].[O;H0;+0:23]=[O;H0;+0:24]>>[*:9]-[CH;+0:10]=[O;H0;+0:21].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:11]-[n+;H0:12]1:[cH;+0:13]:[c;H0;+0:14](-[*:15]):[cH;+0:16]:[cH;+0:17]:[cH;+0:18]:1.[OH2;+0:22].[OH2;+0:23].[OH2;+0:24] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis. | Quaderer R, Omura S, Ikeda H, Cane DE | 2006 Oct 11 | 17017767 |