| ID: | 6.2.1.13 |
|---|---|
| Description: | Acetate--CoA ligase (ADP-forming). |
| Alternative Name: |
Acetyl-CoA synthetase (ADP-forming). Acetate thiokinase. |
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 6.2.1.13 |
| BRENDA Enzyme Link: | BRENDA 6.2.1.13 |
| KEGG Enzyme Link: | KEGG6.2.1.13 |
| BioCyc Enzyme Link: | BioCyc 6.2.1.13 |
| ExPASy Enzyme Link: | ExPASy6.2.1.13 |
| EC2PDB Enzyme Link: | EC2PDB 6.2.1.13 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.2.1.13 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.2.1.13 |
| IntEnz Enzyme Link: | IntEnz 6.2.1.13 |
| MEDLINE Enzyme Link: | MEDLINE 6.2.1.13 |
| RHEA:29843 | ATP + CoA + propanoate = ADP + phosphate + propanoyl-CoA |
| RULE(radius=1) | [*:1]-[SH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:12]-[OH;+0:11].[*:1]-[S;H0;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| RHEA:15081 | acetate + ATP + CoA = acetyl-CoA + ADP + phosphate |
| RULE(radius=1) | [*:1]-[SH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:12]-[OH;+0:11].[*:1]-[S;H0;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase. | Reeves RE, Warren LG, Susskind B, Lo HS | 1977 Jan 25 | 13076 |