5NTC_XENLA
ID 5NTC_XENLA Reviewed; 569 AA.
AC Q6DKB0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000250|UniProtKB:P49902};
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:P49902};
DE EC=3.1.3.99 {ECO:0000250|UniProtKB:P49902};
DE AltName: Full=Cytosolic nucleoside phosphotransferase 5'N {ECO:0000250|UniProtKB:P49902};
DE EC=2.7.1.77 {ECO:0000250|UniProtKB:P49902};
GN Name=nt5c2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Broad specificity cytosolic 5'-nucleotidase that catalyzes
CC the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates.
CC In addition, possesses a phosphotransferase activity by which it can
CC transfer a phosphate from a donor nucleoside monophosphate to an
CC acceptor nucleoside, preferably inosine, deoxyinosine and guanosine.
CC Has the highest activities for IMP and GMP followed by dIMP, dGMP and
CC XMP. Could also catalyze the transfer of phosphates from pyrimidine
CC monophosphates but with lower efficiency. Through these activities
CC regulates the purine nucleoside/nucleotide pools within the cell.
CC {ECO:0000250|UniProtKB:P49902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a
CC 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside;
CC Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053; EC=3.1.3.99;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000250|UniProtKB:D3ZMY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715;
CC Evidence={ECO:0000250|UniProtKB:D3ZMY7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate;
CC Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61194;
CC Evidence={ECO:0000250|UniProtKB:D3ZMY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384;
CC Evidence={ECO:0000250|UniProtKB:D3ZMY7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate;
CC Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57673;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57464; Evidence={ECO:0000250|UniProtKB:D3ZMY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531;
CC Evidence={ECO:0000250|UniProtKB:D3ZMY7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584,
CC ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP;
CC Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596,
CC ChEBI:CHEBI:57673, ChEBI:CHEBI:58053;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:61194; Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588,
CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58053; Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592,
CC ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:60377; Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P49902};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P49902};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49902};
CC -!- ACTIVITY REGULATION: Allosterically activated by various compounds
CC including ATP, 2,3-BPG/2,3-Bisphosphoglyceric acid and Ap4A/P1,P4-
CC bis(5'-adenosyl) tetraphosphate. Binding of an allosteric activator is
CC a prerequisiste to magnesium and substrate binding. Inhibited by
CC inorganic phosphate. {ECO:0000250|UniProtKB:P49902}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P49902}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49902}.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC074446; AAH74446.1; -; mRNA.
DR RefSeq; NP_001086300.1; NM_001092831.1.
DR AlphaFoldDB; Q6DKB0; -.
DR SMR; Q6DKB0; -.
DR DNASU; 444729; -.
DR GeneID; 444729; -.
DR KEGG; xla:444729; -.
DR CTD; 444729; -.
DR Xenbase; XB-GENE-988880; nt5c2.L.
DR OrthoDB; 712212at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 444729; Expressed in brain and 17 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0050484; F:GMP 5'-nucleotidase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050146; F:nucleoside phosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046054; P:dGMP metabolic process; ISS:UniProtKB.
DR GO; GO:0046037; P:GMP metabolic process; ISS:UniProtKB.
DR GO; GO:0046040; P:IMP metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016695; Pur_nucleotidase.
DR PANTHER; PTHR12103; PTHR12103; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..569
FT /note="Cytosolic purine 5'-nucleotidase"
FT /id="PRO_0000310267"
FT REGION 530..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..569
FT /note="Required for tetramer assembly"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT COMPBIAS 549..569
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 52
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 54
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 202
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 206
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 215
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 249
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 250
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 251
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 292
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P49902"
SQ SEQUENCE 569 AA; 66180 MW; E181B6EAF7455227 CRC64;
MTTSWSDRLQ NAADLPANMD RHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF DLTVERLVSI GYPQELLNFV YDPTFPTRGL VFDSTYGNLI KVDAYGNILV
CAHGFNFMRG LETREQYPNK FIQRDDTDRF YILNTLFNLP ETYLLACLVD FFTNCDRYSS
CETGFKDGDL FMSFRSMFQD VRDAVDWVHY KGSLKEKTVE NLPKYVVKDS KLPLLLSRMN
EVGKVFLVTN SDYKYTHKIM TYLFDLPHGP KPDSSHRVWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTNTG KLKIGTYTGP LQHGIVYSGG SSDILCDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRVKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHAHVDIHES ESPMATRNRC SLDFKDSEFK RHHLTRSISE IKPPNLFPQK
PREITHCHDE DDDEEEEEEE EEEEEEEEE
