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phosphoadenosine phosphosulfate reductase family protein
This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases [1]. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) [1,2]. It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase) [3]. [1]. 9261082. Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Savage H, Montoya G, Svensson C, Schwenn JD, Sinning I;. Structure 1997;5:895-906. [2]. 7588765. Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Berendt U, Haverkamp T, Prior A, Schwenn JD;. Eur J Biochem 1995;233:347-356. [3]. 2250719. ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti. Schwedock J, Long SR;. Nature 1990;348:644-647. (from Pfam)
adenylyl/phosphoadenylyl-sulfate reductase
adenylyl/phosphoadenylyl-sulfate reductase catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS)/phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as the electron donor
phosphoadenylyl-sulfate reductase
Catalyzes the reduction of 3'-phosphoadenylyl sulfate into sulfite
phosphoadenosine phosphosulfate reductase
Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite [2].
phosophoadenylyl-sulfate reductase
This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS.
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