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A0A851B6E4 · A0A851B6E4_PICGY

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.

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

    • Name
      Nt5c2_0
    • ORF names
      PICGYM_R01599

Organism names

  • Taxonomic identifier
  • Strain
    • B10K-DU-012-30
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Picathartidae > Picathartes

Accessions

  • Primary accession
    A0A851B6E4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region494-566Disordered
Compositional bias511-527Basic and acidic residues
Compositional bias548-566Acidic residues

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    566
  • Mass (Da)
    65,551
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    C3EA1FB9A7CB23FB3287381C7C83BBDF
MTTSWSDRLQNAADLPANMDGHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFDLTVERLVSIGYPHELLNFVYDPAFPTRGLVFDTHYGNLLKVDAYGNLLVCAHGFNFLRGPETREQYPNKFIQRDDTDRFYILNTLFNLPETYLLACLVDFFTNCDRYTSCETGFKDGDLFMSFRSMFQDVRDAVDWVHYKGSLKEKTLENLEKYVVKDGKLPLLLSRMNEVGKVFLVTNSDYKYTDKIMTYLFDFPHGPKPGSAHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTVTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSALFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEKESPMATRNRTSVDFKDSDYKRHQLTRSISEIKPPNLFPQAPQEITHCHDEDDDEEEEEEEEEEEEE

Features

Showing features for non-terminal residue, compositional bias.

Type
IDPosition(s)Description
Non-terminal residue1
Compositional bias511-527Basic and acidic residues
Compositional bias548-566Acidic residues
Non-terminal residue566

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEKY01025773
EMBL· GenBank· DDBJ
NWI40842.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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