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1.8.4.8: phosphoadenylyl-sulfate reductase (thioredoxin)

This is an abbreviated version!
For detailed information about phosphoadenylyl-sulfate reductase (thioredoxin), go to the full flat file.

Word Map on EC 1.8.4.8

Reaction

adenosine 3',5'-bisphosphate
+
sulfite
+
thioredoxin disulfide
=
3'-phosphoadenylyl sulfate
+
thioredoxin

Synonyms

3'-Phosphoadenosine 5'-phosphosulfate reductase, 3'-Phosphoadenylylsulfate reductase, 4Fe-4S adenylyl sulfate/phosphoadenylyl sulfate reductase, 5'-adenylylsulfate reductase, Adenosine 3'-phosphate 5'-phosphosulfate reductase, adenosine 5'-phosphosulfate reductase, Adenylyl phosphosulfate reductase, APR, APS reductase, CysH1, EC 1.8.99.4, PAdoPS reductase, PAPS reductase, PAPS reductase, thioredoxin dependent, PAPS reductase, thioredoxin-dependent, PAPS sulfotransferase, Phospho-adenylylsulfate (PAPS) reductase, Phospho-adenylylsulfate reductase, Reductase, 3'-phosphoadenosine 5'-phosphosulfate, SNR, Thioredoxin: 3'-phospho-adenylylsulfate reductase, Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.8 phosphoadenylyl-sulfate reductase (thioredoxin)

Crystallization

Crystallization on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.0 A. The enzyme shows striking similarity to the structure of the ATP pyrophosphatase domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold
-
crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate reductase in complex with Escherichia coli thioredoxin 1 determined to 3.0 A resolution, crystals are grown by vapor diffusion in sitting drops