Protein Family Models

This presumed domain is functionally uncharacterised. This domain is found in bacteria. This domain is typically between 53 to 190 amino acids in length. This domain is found associated with Pfam:PF01507. This domain has a conserved KND sequence motif. (from Pfam)

Date:

2024-08-14

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 uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP), contains a C-terminal DUF3440 domain

Date:

2017-12-05