A0A094KPY6 · A0A094KPY6_PODCR

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.

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.

Type
IDPosition(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

    • ORF names
      N338_07816

Organism names

  • Taxonomic identifier
  • Strain
    • BGI_N338
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Mirandornithes > Podicipediformes > Podicipedidae > Podiceps

Accessions

  • Primary accession
    A0A094KPY6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    424
  • Mass (Da)
    48,855
  • Last updated
    2014-11-26 v1
  • Checksum
    9A6A3C3DC25B7056
MTTSWSDRLQNAADLPANMDGHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFDLTVERLVSIGYPHELLNFVYDPAFPTRGLVFDTHYGNLLKVDAYGNLLVCAHGFNFLRGPETRDQYPNKFIQRDDTDRFYILNTLFNLPETYLLACLVDFFTNCDRYTSCETGFKDGDLFMSFRSMFQDVRDAVDWVHYKGSLKEKTLENLEKYVVKDGKLPLLLSRMNEVGKVFLVTNSDYKYTDKIMTYLFDFPHGPKPGSAHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTVTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSALFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue424

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL264666
EMBL· GenBank· DDBJ
KFZ61318.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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