A0A5C6PGU5 · A0A5C6PGU5_9TELE

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 site65Nucleophile
Binding site65Mg2+ (UniProtKB | ChEBI)
Active site67Proton donor
Binding site67GMP (UniProtKB | ChEBI)
Binding site375Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function5'-nucleotidase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functiontransferase activity
Biological ProcessGMP 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
      D4764_11G0001820

Organism names

  • Taxonomic identifier
  • Strain
    • HTHZ2018
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Tetraodontiformes > Tetradontoidea > Tetraodontidae > Takifugu

Accessions

  • Primary accession
    A0A5C6PGU5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region552-586Disordered
Compositional bias572-586Acidic residues

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    586
  • Mass (Da)
    68,131
  • Last updated
    2019-11-13 v1
  • Checksum
    233D3656B043DD20
MIKALLEKRLLQFKMTSWSDRLQNYADLPVNMDGLALKKYRREAHHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFDLTVERLVSIGYPQELLNFVYDPSFPTRGLVFDTLYGNLLKVDTYGNILVCVHGFNFLRGPEIREKYPNKFIQRGDTERFYILNTLFNLPETYLFACLVDFFSNCSRYTSCETGFKDGDLFMSYKSMFQDVRDGVDWVHFKGSLKEKTVENLEKYVVKDSNISFFLPSNKPKLPLLLSRMKEVAKVFLATNSDYKYTEKIMTYLFDFAHGPKPGMPHRPWQSYFDLILVDARKPVFFAEGTVLRQVDTTTGRLKIGTYTGPLQHGIVYSGGSSDIVCDLMGIKGKDIIYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSIFEELQSLDCFLAELYKHLDSSSNERPDISSLQRRIKKITHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHAHVSFIDTESPLATRNRHDVDLKEMECKRHQLTRSVSEIQPPHLYPQTPQEITHCHDEDDDEEEEEEEEE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias572-586Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RHFK02000003
EMBL· GenBank· DDBJ
TWW78061.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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