ID A0A851ZLE4_CALOR Unreviewed; 566 AA. AC A0A851ZLE4; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 02-OCT-2024, entry version 13. 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}; DE Flags: Fragment; GN Name=Nt5c2 {ECO:0000313|EMBL:NXE58792.1}; GN ORFNames=CALORN_R07142 {ECO:0000313|EMBL:NXE58792.1}; OS Calcarius ornatus (Chestnut-collared longspur). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Fringillidae; OC Emberizinae; Emberizini; Calcarius. OX NCBI_TaxID=198940 {ECO:0000313|EMBL:NXE58792.1, ECO:0000313|Proteomes:UP000603627}; RN [1] {ECO:0000313|EMBL:NXE58792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B10K-DU-015-28 {ECO:0000313|EMBL:NXE58792.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXE58792.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-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:NXE58792.1}. 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; WBNL01000006; NXE58792.1; -; Genomic_DNA. DR AlphaFoldDB; A0A851ZLE4; -. DR Proteomes; UP000603627; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProt. 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|PIRSR:PIRSR017434-2}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000603627}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT REGION 494..566 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 511..527 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..566 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 52 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1" FT ACT_SITE 54 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT BINDING 54 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT BINDING 351 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXE58792.1" FT NON_TER 566 FT /evidence="ECO:0000313|EMBL:NXE58792.1" SQ SEQUENCE 566 AA; 65551 MW; E1FED8C359DA87D4 CRC64; MTTSWSDRLQ NAADLPANMD GHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF DLTVERLVSI GYPHELLNFV YDPAFPTRGL VFDTHYGNLL KVDAYGNLLV CAHGFNFLRG PETREQYPNK FIQRDDTDRF YILNTLFNLP ETYLLACLVD FFTNCDRYTS CETGFKDGDL FMSFRSMFQD VRDAVDWVHY KGSLKEKTLE NLEKYVVKDG KLPLLLSRMN EVGKVFLVTN SDYKYTDKIM TYLFDFPHGP KPGSAHRPWQ SYFDLILVDA RKPLFFGEGT VLRQVDTVTG KLKIGTYTGP LQHGIVYSGG SSDTVCDLLG AKGKDILYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSALFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEK ESPMATRNRT SVDFKDSDYK RHQLTRSISE IKPPNLFPQA PQEITHCHDE DDDEEEEEEE EEEEEE //