Q42546 · DPNP1_ARATH

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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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 μM1D-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
IDPosition(s)Description
Active site46Proton acceptor
Binding site71Mg2+ 1 (UniProtKB | ChEBI)
Binding site71Mg2+ 3 (UniProtKB | ChEBI)
Binding site134Mg2+ 1 (UniProtKB | ChEBI)
Binding site134Mg2+ 2 (UniProtKB | ChEBI)
Binding site136Mg2+ 1 (UniProtKB | ChEBI)
Binding site137Mg2+ 2 (UniProtKB | ChEBI)
Active site139Proton acceptor
Binding site139adenosine 3',5'-bisphosphate (UniProtKB | ChEBI)
Binding site235adenosine 3',5'-bisphosphate (UniProtKB | ChEBI)
Binding site235AMP (UniProtKB | ChEBI)
Binding site259adenosine 3',5'-bisphosphate (UniProtKB | ChEBI)
Binding site259AMP (UniProtKB | ChEBI)
Binding site262adenosine 3',5'-bisphosphate (UniProtKB | ChEBI)
Binding site262AMP (UniProtKB | ChEBI)
Binding site276adenosine 3',5'-bisphosphate (UniProtKB | ChEBI)
Binding site276AMP (UniProtKB | ChEBI)
Binding site288adenosine 3',5'-bisphosphate (UniProtKB | ChEBI)
Binding site288AMP (UniProtKB | ChEBI)
Binding site288Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function3'(2'),5'-bisphosphate nucleotidase activity
Molecular Functioninositol-1,4-bisphosphate 1-phosphatase activity
Molecular Functionmetal ion binding
Biological Processabscisic acid-activated signaling pathway
Biological Processsulfate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3'(2'),5'-bisphosphate nucleotidase 1
  • EC number
  • Alternative names
    • 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 1
    • 3'-phosphoadenosine-5'-phosphate phosphatase 1
      (PAP phosphatase 1
      ; PAPase 1
      )
    • DPNPase 1
    • Inositol polyphosphate 1-phosphatase 1
      (IPPase 1)
    • Inositol-1,4-bisphosphate 1-phosphatase 1 (EC:3.1.3.57
      ) . EC:3.1.3.57 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      SAL1
    • Synonyms
      FRY1
    • ORF names
      MBM17.8
    • Ordered locus names
      At5g63980

Organism names

  • Taxonomic identifier
  • Strains
    • cv. C24
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q42546
  • Secondary accessions
    • F4KC73
    • Q0WTT5

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis287-353In fry1-1; abolishes activity.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001425301-3533'(2'),5'-bisphosphate nucleotidase 1

Proteomic databases

Expression

Tissue specificity

Expressed in roots, leaves, stems, flowers and siliques.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    353
  • Mass (Da)
    37,564
  • Last updated
    1996-11-01 v1
  • Checksum
    351EBB6826B93A4A
MAYEKELDAAKKAASLAARLCQKVQKALLQSDVQSKSDKSPVTVADYGSQAVVSLVLEKELSSEPFSLVAEEDSGDLRKDGSQDTLERITKLVNDTLATEESFNGSTLSTDDLLRAIDCGTSEGGPNGRHWVLDPIDGTKGFLRGDQYAVALGLLEEGKVVLGVLACPNLPLASIAGNNKNKSSSDEIGCLFFATIGSGTYMQLLDSKSSPVKVQVSSVENPEEASFFESFEGAHSLHDLSSSIANKLGVKAPPVRIDSQAKYGALSRGDGAIYLRFPHKGYREKIWDHVAGAIVVTEAGGIVTDAAGKPLDFSKGKYLDLDTGIIVANEKLMPLLLKAVRDSIAEQEKASAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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