EC number:1.17.5.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.17 Acting on CH or CH2 groups |
| 1.17.5 With a quinone or similar compound as acceptor |
| ID: | 1.17.5.3 | ||
|---|---|---|---|
| Description: | Formate dehydrogenase-N. | ||
| Alternative Name: |
Nitrate inducible formate dehydrogenase. Formate dehydrogenase N. | ||
| Prosite: | PDOC00392; | ||
| PDB: |
|
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.17.5.3 |
| BRENDA Enzyme Link: | BRENDA 1.17.5.3 |
| KEGG Enzyme Link: | KEGG1.17.5.3 |
| BioCyc Enzyme Link: | BioCyc 1.17.5.3 |
| ExPASy Enzyme Link: | ExPASy1.17.5.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.17.5.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.17.5.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.17.5.3 |
| IntEnz Enzyme Link: | IntEnz 1.17.5.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.17.5.3 |
| RHEA:29063 | a menaquinone + formate + H(+) = a menaquinol + CO2 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[*:7](:[cH;+0:8]:[*:9]):[c;H0;+0:10](:[*:11])-[C;H0;+0:12]-1=[O;H0;+0:13].[*:14]=[CH;+0:15]-[OH;+0:16].[H+;H0:17]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[*:7](:[cH;+0:10]:[*:11]):[c;H0;+0:8](:[*:9]):[c;H0;+0:12]:1-[OH;+0:13].[*:14]=[C;H0;+0:15]=[O;H0;+0:16] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. | Jormakka M, Törnroth S, Byrne B, Iwata S | 2002 Mar 8 | 11884747 |
| RHEA:29067 | formate + H(+) + menaquinone-8 = CO2 + menaquinol-8 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[*:7]:[*:8]-[C;H0;+0:9]-1=[O;H0;+0:10].[*:11]=[CH;+0:12]-[OH;+0:13].[H+;H0:14]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[*:7]:[*:8]:[c;H0;+0:9]:1-[OH;+0:10].[*:11]=[C;H0;+0:12]=[O;H0;+0:13] |
| Reaction |  |
| Core-to-Core |
| RHEA:29071 | a ubiquinone + formate + H(+) = a ubiquinol + CO2 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]=[CH;+0:14]-[OH;+0:15].[H+;H0:16]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[*:10]):[c;H0;+0:11]:1-[OH;+0:12].[*:13]=[C;H0;+0:14]=[O;H0;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The hydrogenases and formate dehydrogenases of Escherichia coli. | Sawers G | 1994 | 7747941 |
| RHEA:48592 | a quinone + formate + H(+) = a quinol + CO2 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]=[CH;+0:14]-[OH;+0:15].[H+;H0:16]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:11](-[OH;+0:12]):[c;H0;+0:9](-[*:10]):[c;H0;+0:7](-[*:8]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:3]:1-[*:4].[*:13]=[C;H0;+0:14]=[O;H0;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli. | Jormakka M, Törnroth S, Abramson J, Byrne B, Iwata S | 2002 Jan | 11752799 |
| The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. | Enoch HG, Lester RL | 1975 Sep 10 | 1099093 |
| Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. | Jormakka M, Törnroth S, Byrne B, Iwata S | 2002 Mar 8 | 11884747 |