EC Tree |
1. Oxidoreductases |
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
ID: | 1.14.13.38 |
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Description: | Anhydrotetracycline 6-monooxygenase. |
Alternative Name: |
ATC oxygenase. Anhydrotetracycline oxygenase. Anhydrotetracycline monooxygenase. |
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 1.14.13.38 |
BRENDA Enzyme Link: | BRENDA 1.14.13.38 |
KEGG Enzyme Link: | KEGG1.14.13.38 |
BioCyc Enzyme Link: | BioCyc 1.14.13.38 |
ExPASy Enzyme Link: | ExPASy1.14.13.38 |
EC2PDB Enzyme Link: | EC2PDB 1.14.13.38 |
ExplorEnz Enzyme Link: | ExplorEnz 1.14.13.38 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.14.13.38 |
IntEnz Enzyme Link: | IntEnz 1.14.13.38 |
MEDLINE Enzyme Link: | MEDLINE 1.14.13.38 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:11976 | anhydrotetracycline + H(+) + NADPH + O2 = 5a,11a-dehydrotetracycline + H2O + NADP(+) |
RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[c;H0;+0:10]1:[c;H0;+0:11](-[OH;+0:12]):[*:13]:[*:14]:[c;H0;+0:15](-[*:16]):[c;H0;+0:17]:1-[*:18].[H+;H0:19].[O;H0;+0:20]=[O;H0;+0:21]>>[*:9]-[C;H0;+0:10]1=[C;H0;+0:17](-[*:18])-[C;H0;+0:15](-[*:16])(-[OH;+0:20])-[*:14]:[*:13]-[C;H0;+0:11]-1=[O;H0;+0:12].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:21] |
Reaction | ![]() |
Core-to-Core | |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Ablation of the otcC gene encoding a post-polyketide hydroxylase from the oxytetracyline biosynthetic pathway in Streptomyces rimosus results in novel polyketides with altered chain length. | Peric-Concha N, Borovicka B, Long PF, Hranueli D, Waterman PG, Hunter IS | 2005 Nov 11 | 16148009 |