Q9XWN7 · NSH1_CAEEL

Function

function

Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Note: Binds 1 Ca2+ ion per monomer.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.295 mMinosine7.037
0.129 mMinosine7.025
0.093 mMadenosine7.037
0.077 mMadenosine7.025
0.164 mMguanosine7.037
0.068 mMguanosine7.025
0.037 mM7-methylguanosine7.025
10.004 mMcytidine7.037
2.843 mMuridine7.037
1.038 mMxanthosine7.037
kcat is 0.79 sec-1 with inosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783).
kcat is 0.203 sec-1 with inosine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:28218438).
kcat is 0.78 sec-1 with adenosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783).
kcat is 0.418 sec-1 with adenosine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:28218438).
kcat is 0.84 sec-1 with guanosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783).
kcat is 0.143 sec-1 with guanosine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:28218438).
kcat is 0.50 sec-1 with cytidine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783).
kcat is 0.002 sec-1 with uridine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783).
kcat is 0.029 sec-1 with xanthosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783).

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site13Proton acceptor
Binding site13Ca2+ (UniProtKB | ChEBI); catalytic
Binding site18Ca2+ (UniProtKB | ChEBI); catalytic
Binding site133Ca2+ (UniProtKB | ChEBI); catalytic
Binding site254Ca2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Molecular Functionadenosine nucleosidase activity
Molecular Functioncalcium ion binding
Molecular Functioninosine nucleosidase activity
Molecular Functionpurine nucleosidase activity
Biological Processpurine nucleoside catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • ORF names
      Y43F8C.13

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q9XWN7

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis42Reduces hydrolysis of inosine, adenosine, and guanosine by a factor of about 14-, 22-, and 10-fold, respectively.
Mutagenesis253Reduces hydrolysis of inosine, adenosine and guanosine by a factor of about 120-fold. May be involved in leaving group activation, acting as a general acid required to protonate the N7 of the purine leaving group.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004572121-338Nucleoside hydrolase

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the IUNH family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    338
  • Mass (Da)
    37,215
  • Last updated
    1999-11-01 v1
  • Checksum
    2F604EA869EBD250
MTVDKVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDDTVSDFFGIDGIGDKPEEFPKVERSDFEGEGKHASLALIDILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYAVGNVDGGSSAEYNFHGDPEAASIVLRRMKCPITIVPWEAFYFESKTHDASVDFSAHLKYGTPLANYLSLATSIGRVKCEANGRQYSYCDEIAVATAIDEDKIAKKSQYLYVDVELNGTKTRGQVVVDWTEQLWSNEEAPNQHTHRRVKFVTSYDVHTVDKWLHAATSGSGKFD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX284605
EMBL· GenBank· DDBJ
CAA21614.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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