ID A0A5C6PGU5_9TELE Unreviewed; 586 AA. AC A0A5C6PGU5; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 29-MAY-2024, entry version 16. DE RecName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000256|ARBA:ARBA00040391}; DE EC=2.7.1.77 {ECO:0000256|ARBA:ARBA00038866}; DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643}; DE EC=3.1.3.99 {ECO:0000256|ARBA:ARBA00012894}; DE AltName: Full=Cytosolic nucleoside phosphotransferase 5'N {ECO:0000256|ARBA:ARBA00042328}; GN ORFNames=D4764_11G0001820 {ECO:0000313|EMBL:TWW78061.1}; OS Takifugu flavidus (sansaifugu). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW78061.1, ECO:0000313|Proteomes:UP000324091}; RN [1] {ECO:0000313|EMBL:TWW78061.1, ECO:0000313|Proteomes:UP000324091} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW78061.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:TWW78061.1}; RA Xiao S.; RT "Chromosome genome assembly for Takifugu flavidus."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00036349}; 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:0000256|ARBA:ARBA00036204}; 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:0000256|ARBA:ARBA00036695}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715; CC Evidence={ECO:0000256|ARBA:ARBA00036695}; 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:0000256|ARBA:ARBA00036089}; 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:0000256|ARBA:ARBA00036953}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719; CC Evidence={ECO:0000256|ARBA:ARBA00036953}; 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:0000256|ARBA:ARBA00036213}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531; CC Evidence={ECO:0000256|ARBA:ARBA00036213}; 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:0000256|ARBA:ARBA00036260}; 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:0000256|ARBA:ARBA00035871}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485; CC Evidence={ECO:0000256|ARBA:ARBA00035871}; 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:0000256|ARBA:ARBA00036911}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380; CC Evidence={ECO:0000256|ARBA:ARBA00036911}; 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:0000256|ARBA:ARBA00036593}; 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:0000256|ARBA:ARBA00036191}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384; CC Evidence={ECO:0000256|ARBA:ARBA00036191}; 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:0000256|ARBA:ARBA00036258}; 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:0000256|ARBA:ARBA00036826}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR017434-2}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC {ECO:0000256|ARBA:ARBA00009589}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TWW78061.1}. 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; RHFK02000003; TWW78061.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5C6PGU5; -. DR Proteomes; UP000324091; Chromosome 11. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0046085; P:adenosine metabolic process; IEA:TreeGrafter. DR GO; GO:0046037; P:GMP metabolic process; IEA:UniProt. DR GO; GO:0046040; P:IMP metabolic process; IEA:TreeGrafter. DR CDD; cd07522; HAD_cN-II; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1. DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1. DR PANTHER; PTHR12103:SF17; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1. DR Pfam; PF05761; 5_nucleotid; 1. DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR017434-2}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000324091}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT REGION 552..586 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 572..586 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 65 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1" FT ACT_SITE 67 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1" FT BINDING 65 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT BINDING 67 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT BINDING 375 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" SQ SEQUENCE 586 AA; 68131 MW; 233D3656B043DD20 CRC64; MIKALLEKRL LQFKMTSWSD RLQNYADLPV NMDGLALKKY RREAHHRVFV NRSLAMEKIK CFGFDMDYTL AVYKSPEYES LGFDLTVERL VSIGYPQELL NFVYDPSFPT RGLVFDTLYG NLLKVDTYGN ILVCVHGFNF LRGPEIREKY PNKFIQRGDT ERFYILNTLF NLPETYLFAC LVDFFSNCSR YTSCETGFKD GDLFMSYKSM FQDVRDGVDW VHFKGSLKEK TVENLEKYVV KDSNISFFLP SNKPKLPLLL SRMKEVAKVF LATNSDYKYT EKIMTYLFDF AHGPKPGMPH RPWQSYFDLI LVDARKPVFF AEGTVLRQVD TTTGRLKIGT YTGPLQHGIV YSGGSSDIVC DLMGIKGKDI IYIGDHIFGD ILKSKKRQGW RTFLVIPELA QELHVWTDKS SIFEELQSLD CFLAELYKHL DSSSNERPDI SSLQRRIKKI THDMDMCYGM MGSLFRSGSR QTLFASQVMR YADLYAASFI NLLYYPFSYL FRAAHVLMPH ESTVEHAHVS FIDTESPLAT RNRHDVDLKE MECKRHQLTR SVSEIQPPHL YPQTPQEITH CHDEDDDEEE EEEEEE //