| ID: | 6.2.1.51 |
|---|---|
| Description: | 4-hydroxyphenylalkanoate adenylyltransferase FadD29. |
| Alternative Name: |
4-hydroxyphenylalkanoate adenylase. |
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 6.2.1.51 |
| BRENDA Enzyme Link: | BRENDA 6.2.1.51 |
| KEGG Enzyme Link: | KEGG6.2.1.51 |
| BioCyc Enzyme Link: | BioCyc 6.2.1.51 |
| ExPASy Enzyme Link: | ExPASy6.2.1.51 |
| EC2PDB Enzyme Link: | EC2PDB 6.2.1.51 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.2.1.51 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.2.1.51 |
| IntEnz Enzyme Link: | IntEnz 6.2.1.51 |
| MEDLINE Enzyme Link: | MEDLINE 6.2.1.51 |
| RHEA:55728 | 19-(4-hydroxyphenyl)nonadecanoate + ATP + holo-[(phenol)carboxyphthiodiolenone synthase] = 19-(4-hydroxyphenyl)nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[*:7]-[SH;+0:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:1]-[OH;+0:2].[*:4]-[P;H0;+0:3](=[*:5])(-[*:6])-[OH;+0:12].[*:7]-[S;H0;+0:8]-[C;H0;+0:10](=[*:9])-[*:11] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum. | Vergnolle O, Chavadi SS, Edupuganti UR, Mohandas P, Chan C, Zeng J, Kopylov M, Angelo NG, Warren JD, Soll CE, Quadri LE | 2015 Mar | 25561717 |
| Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis. | Siméone R, Léger M, Constant P, Malaga W, Marrakchi H, Daffé M, Guilhot C, Chalut C | 2010 Jun | 20553505 |
| RHEA:55720 | 17-(4-hydroxyphenyl)heptadecanoate + ATP + holo-[(phenol)carboxyphthiodiolenone synthase] = 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[*:7]-[SH;+0:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:1]-[OH;+0:2].[*:4]-[P;H0;+0:3](=[*:5])(-[*:6])-[OH;+0:12].[*:7]-[S;H0;+0:8]-[C;H0;+0:10](=[*:9])-[*:11] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum. | Vergnolle O, Chavadi SS, Edupuganti UR, Mohandas P, Chan C, Zeng J, Kopylov M, Angelo NG, Warren JD, Soll CE, Quadri LE | 2015 Mar | 25561717 |
| Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis. | Siméone R, Léger M, Constant P, Malaga W, Marrakchi H, Daffé M, Guilhot C, Chalut C | 2010 Jun | 20553505 |