Protein Family Models

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)

Date:

2024-10-16

phosphoadenosine phosphosulfate reductase family protein is involved in the assimilation of sulfate and it catalyzes the reduction of 3'-phospho-adenylylsulfate (PAPS) or 5'-adenylyl sulfate to sulfite and phospho-adenosine-phosphate (PAP) or AMP using thioredoxin as the electron donor

Date:

2017-07-05

Catalyzes the reduction of 3'-phosphoadenylyl sulfate into sulfite

Date:

2021-07-22

This model describes recently identified adenosine 5'-phosphosulfate (APS) reductase activity found in sulfate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulfate (PAPS) reductases found in bacteria and fungi [1]. Homologous to PAPS reductase in enterobacteria, cyanobacteria, and yeast, APS reductase here clusters with, and demonstrates greater homology to plant APS reductase. Additionally, the presence of two conserved C-terminal motifs (CCXXRKXXPL & SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster [2].

Date:

2024-05-30

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.

Gene:

cysH

Date:

2021-04-27