ID A0A6J2PKV2_COTGO Unreviewed; 562 AA. AC A0A6J2PKV2; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 27-NOV-2024, entry version 20. 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 Name=nt5c2 {ECO:0000313|RefSeq:XP_029286683.1}; OS Cottoperca gobio (Frogmouth) (Aphritis gobio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca. OX NCBI_TaxID=56716 {ECO:0000313|Proteomes:UP000504630, ECO:0000313|RefSeq:XP_029286683.1}; RN [1] {ECO:0000313|RefSeq:XP_029286683.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (AUG-2024) to UniProtKB. 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:0000256|ARBA:ARBA00046009}. CC -!- CATALYTIC ACTIVITY: CC Reaction=inosine + AMP = IMP + adenosine; 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=inosine + CMP = 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=inosine + GMP = 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=IMP + H2O = 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=XMP + H2O = xanthosine + phosphate; 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 ribonucleoside + a 2'-deoxyribonucleoside 5'-phosphate; 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 = uridine + IMP; 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 --------------------------------------------------------------------------- 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 RefSeq; XP_029286683.1; XM_029430823.1. DR AlphaFoldDB; A0A6J2PKV2; -. DR KEGG; cgob:115007821; -. DR InParanoid; A0A6J2PKV2; -. DR OrthoDB; 3626840at2759; -. DR Proteomes; UP000504630; Chromosome 1. 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:0046037; P:GMP metabolic process; IEA:UniProt. DR CDD; cd07522; HAD_cN-II; 1. DR FunFam; 3.40.50.1000:FF:000021; NT5C2 isoform 1; 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:UP000504630}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT REGION 531..562 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..562 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" SQ SEQUENCE 562 AA; 65198 MW; 46F01AF7841AC5A4 CRC64; MTTSWSDRLQ NYADLPANMD GVTMKKYRRE PYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFV YDPSFPTRGL VFDTMYGNLL KVDAYGNILV CVHGFNFLRG PEIRERYPNK FIQRDDTERF YILNTLFNLP ETYLFACLVD FFSNCDRYTS CESGFKNGDL FMSYKSMFQD VRDAVDWVHF KGTLKEKTVE NLEKYVVRDG KLPLLLSRMN EVAKVFLATN SDYKYTDKIM NYLFDFPHGP KPGTSHRPWQ SYFDLILADA RKPLFFGEGT VLRQVDTTTG RLKIGTYTGP LQHGIVYSGG SSDIVCDLLG AKGKDIVYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQGLDIFLA ELYKHLDSSS NERPDISTIQ RRVKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHAHVDIDME SPLATRNRTH CSDCKDLECK RNQLTRSFSE IKPPNLFPQT PQEITHCHDE DDDEEEEEEE EE //