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IPR002500 is a Phosphoadenosine phosphosulphate reductase.
<p>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 [[cite:PUB00005294]].</p> <p>A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold [[cite:PUB00005294]].</p> <p>The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) [[cite:PUB00005294], [cite:PUB00001462]]. It is also found in NodP nodulation protein P from Rhizobium meliloti (Sinorhizobium meliloti) which has ATP sulphurylase activity (sulphate adenylate transferase) [[cite:PUB00004086]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | FAD synthetase [Medicago truncatula] gi|357510801|ref|XP_003625689.1| | 13 | ||
| – | PREDICTED: 5'-adenylylsulfate reductase 3, chloroplastic-like [Glycine max] gi|356521997|ref|XP_003529636.1| | 24 | ||
| – | PREDICTED: 5'-adenylylsulfate reductase 1, chloroplastic-like [Cicer arietinum] gi|502079145|ref|XP_004486168.1| | 18 | ||
| – | Phosphoadenosine phosphosulfate reductase family protein; TAIR: AT5G03430.1 phosphoadenosine phosphosulfate (PAPS) reductase family protein; Swiss-Prot: sp|O74841|FAD1_SCHPO Probable FAD synthase; TrEMBL-Plants: tr|I1NAB5|I1NAB5_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0688100 | 14 | ||
| – | Phosphoadenosine phosphosulfate reductase family protein; TAIR: AT5G03430.1 phosphoadenosine phosphosulfate (PAPS) reductase family protein; Swiss-Prot: sp|O74841|FAD1_SCHPO Probable FAD synthase; TrEMBL-Plants: tr|I1NAB5|I1NAB5_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0688100 | 14 | ||
| – | 5'-adenylylsulfate reductase; TAIR: AT4G21990.1 APS reductase 3; Swiss-Prot: sp|P92980|APR3_ARATH 5'-adenylylsulfate reductase 3, chloroplastic; TrEMBL-Plants: tr|I3S182|I3S182_LOTJA Uncharacterized protein; Found in the gene: LotjaGi4g1v0013600 | 20 | ||
| – | 5'-adenylylsulfate reductase; TAIR: AT4G21990.1 APS reductase 3; Swiss-Prot: sp|P92980|APR3_ARATH 5'-adenylylsulfate reductase 3, chloroplastic; TrEMBL-Plants: tr|A0A072V4H5|A0A072V4H5_MEDTR 5'-adenylylsulfate reductase; Found in the gene: LotjaGi6g1v0294100 | 19 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 14.29 |