Q42546 · DPNP1_ARATH
- Protein3'(2'),5'-bisphosphate nucleotidase 1
- GeneSAL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids353 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphatase that converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. May play a role in the biosynthesis of sulfate conjugates and RNA processing. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. Could be considered as a negative regulator of abscisic acid (ABA)- and stress-responsive genes, through modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt tolerance. Acts as a suppressor of virus- and transgene-induced silencing.
Miscellaneous
Mutation in the FRY1 gene results in super-induction of abscisic acid (ABA)- and stress-responsive genes, due to inositol 1,4,5-trisphosphate (IP3) accumulation.
Substrate preference is adenosine 3'-phosphate 5'-phosphosulfate (PAPS) > 3'-phosphoadenosine 5'-phosphate (PAP) = 2'-phosphoadenosine 5'-phosphate > inositol 1,4-bisphosphate = inositol 1,4,5-trisphosphate. No activity observed against 3' or 5'-AMP, inositol 1-phosphate, ATP, fructose 1,6-bisphosphate, or inositol hexaphosphate.
Catalytic activity
- 3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol 3,4-bisphosphate + phosphateThis reaction proceeds in the forward direction.
Cofactor
Activity regulation
Inhibited non-competitively by Li+ (IC50=0.20 mM) and Na+ (IC50=200 mM).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
90 μM | 1D-myo-inositol 1,4-bisphosphate |
KM for adenosine 3',5'-bisphosphate is between 2 and 10 uM.
pH Dependence
Optimum pH is 7.5.
Pathway
Signal transduction; phosphatidylinositol signaling pathway.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 46 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 71 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 71 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 134 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 134 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 136 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 137 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 139 | Proton acceptor | ||||
Sequence: T | ||||||
Binding site | 139 | adenosine 3',5'-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 235 | adenosine 3',5'-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 235 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 259 | adenosine 3',5'-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 259 | AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 262 | adenosine 3',5'-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 262 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 276 | adenosine 3',5'-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 276 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 288 | adenosine 3',5'-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3'(2'),5'-bisphosphate nucleotidase activity | |
Molecular Function | inositol-1,4-bisphosphate 1-phosphatase activity | |
Molecular Function | metal ion binding | |
Biological Process | abscisic acid-activated signaling pathway | |
Biological Process | sulfate assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3'(2'),5'-bisphosphate nucleotidase 1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ42546
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 287-353 | In fry1-1; abolishes activity. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000142530 | 1-353 | 3'(2'),5'-bisphosphate nucleotidase 1 | |||
Sequence: MAYEKELDAAKKAASLAARLCQKVQKALLQSDVQSKSDKSPVTVADYGSQAVVSLVLEKELSSEPFSLVAEEDSGDLRKDGSQDTLERITKLVNDTLATEESFNGSTLSTDDLLRAIDCGTSEGGPNGRHWVLDPIDGTKGFLRGDQYAVALGLLEEGKVVLGVLACPNLPLASIAGNNKNKSSSDEIGCLFFATIGSGTYMQLLDSKSSPVKVQVSSVENPEEASFFESFEGAHSLHDLSSSIANKLGVKAPPVRIDSQAKYGALSRGDGAIYLRFPHKGYREKIWDHVAGAIVVTEAGGIVTDAAGKPLDFSKGKYLDLDTGIIVANEKLMPLLLKAVRDSIAEQEKASAL |
Proteomic databases
Expression
Tissue specificity
Expressed in roots, leaves, stems, flowers and siliques.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length353
- Mass (Da)37,564
- Last updated1996-11-01 v1
- Checksum351EBB6826B93A4A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U40433 EMBL· GenBank· DDBJ | AAC49263.1 EMBL· GenBank· DDBJ | mRNA | ||
AY034894 EMBL· GenBank· DDBJ | AAK58887.1 EMBL· GenBank· DDBJ | mRNA | ||
AB019227 EMBL· GenBank· DDBJ | BAA96901.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED97825.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT005993 EMBL· GenBank· DDBJ | AAO64928.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227460 EMBL· GenBank· DDBJ | BAE99463.1 EMBL· GenBank· DDBJ | mRNA |