A0A852MN51 · A0A852MN51_9PASS

  • Protein
    Cytosolic purine 5'-nucleotidase
  • Gene
    Nt5c2_0
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine. Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP. Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency. Through these activities regulates the purine nucleoside/nucleotide pools within the cell.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • inosine + AMP = IMP + adenosine
  • inosine + CMP = cytidine + IMP
  • GMP + H2O = guanosine + phosphate
    This reaction proceeds in the forward direction.
  • inosine + GMP = guanosine + IMP
  • IMP + H2O = inosine + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.99 (UniProtKB | ENZYME | Rhea)
  • XMP + H2O = xanthosine + phosphate
    This reaction proceeds in the forward direction.
  • a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a ribonucleoside + a 2'-deoxyribonucleoside 5'-phosphate
    EC:2.7.1.77 (UniProtKB | ENZYME | Rhea)
  • a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.5 (UniProtKB | ENZYME | Rhea)
  • dGMP + H2O = 2'-deoxyguanosine + phosphate
    This reaction proceeds in the forward direction.
  • dGMP + inosine = 2'-deoxyguanosine + IMP
  • dIMP + H2O = 2'-deoxyinosine + phosphate
    This reaction proceeds in the forward direction.
  • dIMP + inosine = 2'-deoxyinosine + IMP
  • inosine + UMP = uridine + IMP

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site52Nucleophile
Binding site52Mg2+ (UniProtKB | ChEBI)
Active site54Proton donor
Binding site54GMP (UniProtKB | ChEBI)
Binding site351Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function5'-nucleotidase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functiontransferase activity
Biological Processadenosine metabolic process
Biological ProcessGMP metabolic process
Biological ProcessIMP metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytosolic purine 5'-nucleotidase
  • EC number
  • Alternative names
    • Cytosolic nucleoside phosphotransferase 5'N

Gene names

    • Name
      Nt5c2_0
    • ORF names
      PTEMEL_R03064

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B10K-IZ-033-77
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Sylvioidea > Timaliidae > Pteruthius

Accessions

  • Primary accession
    A0A852MN51

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region528-562Disordered
Compositional bias548-562Acidic residues

Sequence similarities

Belongs to the 5'(3')-deoxyribonucleotidase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    562
  • Mass (Da)
    65,035
  • Last updated
    2021-09-29 v1
  • Checksum
    19DA87D4EE9402C9
MTTSWSDRLQNAADLPANMDGHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFDLTVERLVSIGYPHELLNFVYDPAFPTRGLVFDTHYGNLLKVDAYGNLLVCAHGFNFLRGPETREQYPNKFIQRDDTDRFYILNTLFNLPETYLLACLVDFFTNCDRYTSCETGFKDGDLFMSFRSMFQDVRDAVDWVHYKGSLKEKTLENLEKYVVKDGKLPLLLSRMNEVGKVFLVTNSDYKYTDKIMTYLFDFPHGPKPGSAHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTVTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSALFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEKESPMATRNRTSVDFKDSDYKRHQLTRSISEIKPPNLFPQAPQEITHCHDEDDDEEEEEEEEE

Features

Showing features for non-terminal residue, compositional bias.

TypeIDPosition(s)Description
Non-terminal residue1
Compositional bias548-562Acidic residues
Non-terminal residue562

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEIY01000053
EMBL· GenBank· DDBJ
NXY01935.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp