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InterPro: IPR011798 Adenylylsulphate reductase, thioredoxin dependent

Protein matches Help

UniProtKB

Matches:

393 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011798 APS_reductase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR02055	APS_reductase	393
Signatures in BioMart

InterPro Relationships Help

Parent

IPR004511 Phosphoadenosine phosphosulphate reductase CysH-type

GO Term annotation Help

Process

GO:0019344 cysteine biosynthetic process
GO:0055114 oxidation reduction

Function

GO:0004604 phosphoadenylyl-sulfate reductase (thioredoxin) activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry describes recently identified adenosine 5'-phosphosulphate (APS) reductase activity found in sulphate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulphate (PAPS) reductases found in bacteria and fungi. 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 and SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster.

Database links Help

Enzyme: EC:1.8.4.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011798

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O05927 Phosphoadenosine phosphosulfate reductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011798	Adenylylsulphate reductase, thioredoxin dependent
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR004511	Phosphoadenosine phosphosulphate reductase CysH-type
IPR002500	Phosphoadenosine phosphosulphate reductase
	PDB Chain
	ModBase

Publications Help

Additional Reading Open in usermanual
	Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR. 5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria. J. Biol. Chem. 277 2002 32606-15 [PubMed: 12072441] http://dx.doi.org/10.1074/jbc.M204613200
	Abola AP, Willits MG, Wang RC, Long SR. Reduction of adenosine-5'-phosphosulfate instead of 3'-phosphoadenosine-5'-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae. J. Bacteriol. 181 1999 5280-7 [PubMed: 10464198] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=10464198&action=stream&blobtype=pdf
	Kopriva S, Buchert T, Fritz G, Suter M, Benda R, Schunemann V, Koprivova A, Schurmann P, Trautwein AX, Kroneck PM, Brunold C. The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation. J. Biol. Chem. 277 2002 21786-91 [PubMed: 11940598] http://dx.doi.org/10.1074/jbc.M202152200
	Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T. Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria. J. Bacteriol. 182 2000 135-42 [PubMed: 10613872] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=10613872

InterPro 23.1