5NTC_CHICK
ID 5NTC_CHICK Reviewed; 569 AA.
AC Q5ZIZ4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000305|PubMed:6060459};
DE EC=3.1.3.5 {ECO:0000269|PubMed:6060459};
DE EC=3.1.3.99 {ECO:0000269|PubMed:6060459};
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; ORFNames=RCJMB04_22h21;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=6060459; DOI=10.1016/0005-2744(67)90081-2;
RA Itoh R., Mitsui A., Tsushima K.;
RT "5'-nucleotidase of chicken liver.";
RL Biochim. Biophys. Acta 146:151-159(1967).
CC -!- FUNCTION: Broad specificity cytosolic 5'-nucleotidase that catalyzes
CC the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates
CC (PubMed:6060459). In addition, possesses a phosphotransferase activity
CC by which it can transfer a phosphate from a donor nucleoside
CC monophosphate to an acceptor nucleoside, preferably inosine,
CC deoxyinosine and guanosine (By similarity). Has the highest activities
CC for IMP and GMP followed by dIMP, dGMP and XMP (PubMed:6060459). Could
CC also catalyze the transfer of phosphates from pyrimidine monophosphates
CC but with lower efficiency (By similarity). Through these activities
CC regulates the purine nucleoside/nucleotide pools within the cell
CC (PubMed:6060459). {ECO:0000250|UniProtKB:P49902,
CC ECO:0000269|PubMed:6060459}.
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:0000269|PubMed:6060459};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485;
CC Evidence={ECO:0000305|PubMed:6060459};
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:0000269|PubMed:6060459};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719;
CC Evidence={ECO:0000305|PubMed:6060459};
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:0000269|PubMed:6060459};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715;
CC Evidence={ECO:0000305|PubMed:6060459};
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:0000269|PubMed:6060459};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380;
CC Evidence={ECO:0000305|PubMed:6060459};
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=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57464; Evidence={ECO:0000269|PubMed:6060459};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531;
CC Evidence={ECO:0000305|PubMed:6060459};
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:0000269|PubMed:6060459};
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 (By similarity). Inhibited by inosine, guanosine,
CC p-chloromercuribenzoate and NaF (PubMed:6060459).
CC {ECO:0000250|UniProtKB:P49902, ECO:0000269|PubMed:6060459}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for IMP {ECO:0000269|PubMed:6060459};
CC KM=1.3 mM for GMP {ECO:0000269|PubMed:6060459};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:6060459};
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}.
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DR EMBL; AJ720640; CAG32299.1; -; mRNA.
DR RefSeq; NP_001026405.1; NM_001031234.1.
DR AlphaFoldDB; Q5ZIZ4; -.
DR SMR; Q5ZIZ4; -.
DR STRING; 9031.ENSGALP00000013294; -.
DR PaxDb; Q5ZIZ4; -.
DR GeneID; 423871; -.
DR KEGG; gga:423871; -.
DR CTD; 22978; -.
DR VEuPathDB; HostDB:geneid_423871; -.
DR eggNOG; KOG2469; Eukaryota.
DR InParanoid; Q5ZIZ4; -.
DR PhylomeDB; Q5ZIZ4; -.
DR Reactome; R-GGA-421178; Urate synthesis.
DR PRO; PR:Q5ZIZ4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0050484; F:GMP 5'-nucleotidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; IDA: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:0046085; P:adenosine metabolic process; IBA:GO_Central.
DR GO; GO:0046054; P:dGMP metabolic process; ISS:UniProtKB.
DR GO; GO:0046037; P:GMP metabolic process; IDA:UniProtKB.
DR GO; GO:0046040; P:IMP metabolic process; IDA: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 1: Evidence at protein 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_0000310266"
FT REGION 527..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 548..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; 65894 MW; C8FD122625879CB6 CRC64;
MTTSWSDRLQ NAADLPANMD GHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF DLTVERLVSI GYPHELLNFV YDPAFPTRGL VFDTHYGNLL KVDAYGNLLV
CAHGFNFLRG PETRDQYPNK 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 VEEEEEEEE
