spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR002500 Phosphoadenosine phosphosulphate reductase

Protein matchesHelp
UniProtKB
Matches:
2682 proteins
AccessionHelp IPR002500 PAPS_reduct
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
Children IPR004511 Phosphoadenosine phosphosulphate reductase CysH-type
Found in IPR004508 Thioredoxin-independent 5'-adenylylsulphate reductase
IPR011784 Sulphate adenylyltransferase, small subunit
IPR011800 Phosphoadenosine phosphosulphate reductase thioredoxin
IPR012183 FAD synthetase, molybdopterin binding
IPR017598 Putative sulfurtransferase DndC
GO Term annotationHelp
Process GO:0008152 metabolic process
Function GO:0016740 transferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes or PAPS sulphotransferase. 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 meliloti (Sinorhizobium meliloti) which has ATP sulphurylase activity (sulphate adenylate transferase) [3].

Structural linksHelp
SCOP: c.26.2.2
CATH: 3.40.50.620
Database linksHelp
PANDIT: PF01507
Blocks: IPB002500
Pfam Clan: CL0039.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002500 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P18408 Phosphoadenosine phosphosulfate reductase

P92979 5'-adenylylsulfate reductase 1, chloroplastic

Q22017 Probable FAD synthetase

Q8NFF5 FAD synthetase

Q8R123 FAD synthetase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
IPR004508 Thioredoxin-independent 5'-adenylylsulphate reductase
IPR001453 Molybdopterin binding
IPR012336 Thioredoxin-like fold
IPR002500 Phosphoadenosine phosphosulphate reductase
IPR017936 Thioredoxin-like
IPR013766 Thioredoxin domain
IPR012335 Thioredoxin fold
IPR011800 Phosphoadenosine phosphosulphate reductase thioredoxin
IPR012183 FAD synthetase, molybdopterin binding
IPR004511 Phosphoadenosine phosphosulphate reductase CysH-type
PDB Chain
ModBase
SWISS-MODEL

PublicationsHelp
1. Savage H, Montoya G, Svensson C, Schwenn JD, Sinning I.
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
Structure 5 895-906 1997 [PubMed: 9261082]
http://dx.doi.org/10.1016/S0969-2126(97)00244-X
2. Berendt U, Haverkamp T, Prior A, Schwenn JD.
Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis.
Eur. J. Biochem. 233 347-56 1995 [PubMed: 7588765]
http://dx.doi.org/10.1111/j.1432-1033.1995.347_1.x
3. Schwedock J, Long SR.
ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti.
Nature 348 644-7 1990 [PubMed: 2250719]
http://dx.doi.org/10.1038/348644a0

Additional ReadingHelp
Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR.
Molecular basis for G protein control of the prokaryotic ATP sulfurylase.
Mol. Cell 21 2006 109-22 [PubMed: 16387658]
http://dx.doi.org/10.1016/j.molcel.2005.10.034
spacer
spacer
InterPro 23.1