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}.
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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
//