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Links from Protein

Items: 7

1.

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)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Date:
2024-10-16
Family Accession:
NF013658.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

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

Date:
2024-06-26
Family Accession:
10792199
Method:
Sparcle
5.

phosphoadenylyl-sulfate reductase

Catalyzes the reduction of 3'-phosphoadenylyl sulfate into sulfite

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Molecular Function:
phosphoadenylyl-sulfate reductase (thioredoxin) activity (GO:0004604)
Biological Process:
sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (GO:0019379)
Date:
2021-07-22
Family Accession:
NF002537.0
Method:
HMM
6.

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].

Gene:
cysH
GO Terms:
Molecular Function:
phosphoadenylyl-sulfate reductase (thioredoxin) activity (GO:0004604)
Biological Process:
sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (GO:0019379)
Date:
2021-04-27
Family Accession:
TIGR02057.1
Method:
HMM
7.

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.

Gene:
cysH
GO Terms:
Molecular Function:
phosphoadenylyl-sulfate reductase (thioredoxin) activity (GO:0004604)
Biological Process:
sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (GO:0019379)
Date:
2021-04-27
Family Accession:
TIGR00434.1
Method:
HMM
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