Enzyme

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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;

3D structure

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References

External Links

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
MSA:

1.8.7.2;

Phylogenetic Tree:

1.8.7.2;

Uniprot:
M-CSA:
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
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References

TitleAuthorsDatePubMed 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 MK1996 Sep 38784198
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 P1995 Jul 17628465
Regulation of CO2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development.Buchanan BB1991 Jul1910303