Enzyme

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EC Tree
     1. Oxidoreductases
        1.8 Acting on a sulfur group of donors
            1.8.4 With a disulfide as acceptor
ID:1.8.4.10
Description:Adenylyl-sulfate reductase (thioredoxin).
Alternative Name: Thioredoxin-dependent 5'-adenylylsulfate reductase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.8.4.10
BRENDA Enzyme Link: BRENDA 1.8.4.10
KEGG Enzyme Link: KEGG1.8.4.10
BioCyc Enzyme Link: BioCyc 1.8.4.10
ExPASy Enzyme Link: ExPASy1.8.4.10
EC2PDB Enzyme Link: EC2PDB 1.8.4.10
ExplorEnz Enzyme Link: ExplorEnz 1.8.4.10
PRIAM enzyme-specific profiles Link: PRIAM 1.8.4.10
IntEnz Enzyme Link: IntEnz 1.8.4.10
MEDLINE Enzyme Link: MEDLINE 1.8.4.10
MSA:

1.8.4.10;

Phylogenetic Tree:

1.8.4.10;

Uniprot:
M-CSA:
RHEA:21976 [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S;H0;+0:4]-[S;H0;+0:5]-[*:6].[*:7]=[S;H0;+0:8](-[*:9])-[OH;+0:10].[H+;H0:11].[H+;H0:12]>>[*:1]-[O;H0;+0:2]-[S;H0;+0:8](=[*:7])(-[*:9])=[O;H0;+0:10].[*:3]-[SH;+0:4].[*:6]-[SH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria.Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T2000 Jan10613872