EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.7 With an iron-sulfur protein as acceptor |
ID: | 1.8.7.2 |
---|---|
Description: | Ferredoxin:thioredoxin reductase. |
Cath: | 3.90.460.10; |
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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 1.8.7.2 |
BRENDA Enzyme Link: | BRENDA 1.8.7.2 |
KEGG Enzyme Link: | KEGG1.8.7.2 |
BioCyc Enzyme Link: | BioCyc 1.8.7.2 |
ExPASy Enzyme Link: | ExPASy1.8.7.2 |
EC2PDB Enzyme Link: | EC2PDB 1.8.7.2 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.7.2 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.7.2 |
IntEnz Enzyme Link: | IntEnz 1.8.7.2 |
MEDLINE Enzyme Link: | MEDLINE 1.8.7.2 |
RHEA:42336 | [thioredoxin]-disulfide + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [2Fe-2S]-[ferredoxin] |
RULE(radius=1) | [*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[S;H0;+0:8]-[S;H0;+0:9]-[*:10].[H+;H0:11].[H+;H0:12]>>[*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:10]-[SH;+0:9].[*:7]-[SH;+0:8] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters. | Staples CR, Ameyibor E, Fu W, Gardet-Salvi L, Stritt-Etter AL, Schürmann P, Knaff DB, Johnson MK | 1996 Sep 3 | 8784198 |
Amino acid sequence of spinach ferredoxin:thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe-4S] cluster. | Chow LP, Iwadate H, Yano K, Kamo M, Tsugita A, Gardet-Salvi L, Stritt-Etter AL, Schürmann P | 1995 Jul 1 | 7628465 |
Regulation of CO2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development. | Buchanan BB | 1991 Jul | 1910303 |