ID: | 2.1.1.335 |
---|---|
Description: | 4-amino-anhydrotetracycline N(4)-methyltransferase. |
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 2.1.1.335 |
BRENDA Enzyme Link: | BRENDA 2.1.1.335 |
KEGG Enzyme Link: | KEGG2.1.1.335 |
BioCyc Enzyme Link: | BioCyc 2.1.1.335 |
ExPASy Enzyme Link: | ExPASy2.1.1.335 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.335 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.335 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.335 |
IntEnz Enzyme Link: | IntEnz 2.1.1.335 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.335 |
MSA: | |
---|---|
Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:50768 | 4-methylamino-4-dedimethylamino-anhydrotetracycline + S-adenosyl-L-methionine = anhydrotetracycline + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[NH;+0:2]-[*:3].[*:4]-[S+;H0:5](-[*:6])-[CH3;+0:7]>>[*:1]-[N;H0;+0:2](-[*:3])-[CH3;+0:7].[*:4]-[S;H0;+0:5]-[*:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. | Zhang W, Watanabe K, Cai X, Jung ME, Tang Y, Zhan J | 2008 May 14 | 18422316 |
RHEA:50764 | 4-amino-4-dedimethylamino-anhydrotetracycline + S-adenosyl-L-methionine = 4-methylamino-4-dedimethylamino-anhydrotetracycline + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[NH;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. | Zhang W, Watanabe K, Cai X, Jung ME, Tang Y, Zhan J | 2008 May 14 | 18422316 |