EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.98 With other, known, physiological acceptors |
ID: | 1.8.98.4 |
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Description: | Coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase. |
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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 1.8.98.4 |
BRENDA Enzyme Link: | BRENDA 1.8.98.4 |
KEGG Enzyme Link: | KEGG1.8.98.4 |
BioCyc Enzyme Link: | BioCyc 1.8.98.4 |
ExPASy Enzyme Link: | ExPASy1.8.98.4 |
EC2PDB Enzyme Link: | EC2PDB 1.8.98.4 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.98.4 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.98.4 |
IntEnz Enzyme Link: | IntEnz 1.8.98.4 |
MEDLINE Enzyme Link: | MEDLINE 1.8.98.4 |
RHEA:55744 | coenzyme B + coenzyme M + 4 H(+) + 2 oxidized coenzyme F420-(gamma-Glu)(n) + 2 reduced [2Fe-2S]-[ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 reduced coenzyme F420-(gamma-Glu)(n) |
RULE(radius=1) | [*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[SH;+0:8].[*:9]-[SH;+0:10].[*:11]-[n;H0;+0:12]1:[*:13]:[*:14]:[cH;+0:15]:[c;H0;+0:16](:[*:17])-[c;H0;+0:18]:1:[n;H0;+0:19]:[*:20].[*:21]-[n;H0;+0:22]1:[*:23]:[*:24]:[cH;+0:25]:[c;H0;+0:26](:[*:27])-[c;H0;+0:28]:1:[n;H0;+0:29]:[*:30].[H+;H0:31].[H+;H0:32].[H+;H0:33].[H+;H0:34]>>[*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:11]-[N;H0;+0:12]1-[*:13]:[*:14]-[CH2;+0:15]-[c;H0;+0:16](:[*:17]):[c;H0;+0:18]-1:[nH;+0:19]:[*:20].[*:21]-[N;H0;+0:22]1-[*:23]:[*:24]-[CH2;+0:25]-[c;H0;+0:26](:[*:27]):[c;H0;+0:28]-1:[nH;+0:29]:[*:30].[*:9]-[S;H0;+0:10]-[S;H0;+0:8]-[*:7] |
Reaction | ![]() |
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Core-to-Core |
Title | Authors | Date | PubMed ID |
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A Ferredoxin- and F420H2-Dependent, Electron-Bifurcating, Heterodisulfide Reductase with Homologs in the Domains Bacteria and Archaea. | Yan Z, Wang M, Ferry JG | 2017 Feb 7 | 28174314 |