5NTC_BOVIN
ID 5NTC_BOVIN Reviewed; 560 AA.
AC O46411;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000305|PubMed:9371705};
DE EC=3.1.3.5 {ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705};
DE EC=3.1.3.99 {ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705};
DE AltName: Full=Cytosolic IMP/GMP-specific 5'-nucleotidase {ECO:0000303|PubMed:9371705};
DE AltName: Full=Cytosolic nucleoside phosphotransferase 5'N {ECO:0000305|PubMed:9371705};
DE EC=2.7.1.77 {ECO:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705};
GN Name=NT5C2 {ECO:0000250|UniProtKB:P49902};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Thymus;
RX PubMed=9371705; DOI=10.1042/bj3280483;
RA Allegrini S., Pesi R., Tozzi M.G., Fiol C.J., Johnson R.B., Eriksson S.;
RT "Bovine cytosolic IMP/GMP-specific 5'-nucleotidase: cloning and expression
RT of active enzyme in Escherichia coli.";
RL Biochem. J. 328:483-487(1997).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8031149; DOI=10.1006/abbi.1994.1282;
RA Pesi R., Turriani M., Allegrini S., Scolozzi C., Camici M., Ipata P.L.,
RA Tozzi M.G.;
RT "The bifunctional cytosolic 5'-nucleotidase: regulation of the
RT phosphotransferase and nucleotidase activities.";
RL Arch. Biochem. Biophys. 312:75-80(1994).
CC -!- FUNCTION: Broad specificity cytosolic 5'-nucleotidase that catalyzes
CC the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates
CC (PubMed:9371705, PubMed:8031149). In addition, possesses a
CC phosphotransferase activity by which it can transfer a phosphate from a
CC donor nucleoside monophosphate to an acceptor nucleoside, preferably
CC inosine, deoxyinosine and guanosine (PubMed:9371705, PubMed:8031149).
CC Has the highest activities for IMP and GMP followed by dIMP, dGMP and
CC XMP (PubMed:9371705, PubMed:8031149). Could also catalyze the transfer
CC of phosphates from pyrimidine monophosphates but with lower efficiency
CC (PubMed:9371705, PubMed:8031149). Through these activities regulates
CC the purine nucleoside/nucleotide pools within the cell (PubMed:9371705,
CC PubMed:8031149). {ECO:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705}.
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:8031149, ECO:0000269|PubMed:9371705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485;
CC Evidence={ECO:0000305|PubMed:9371705};
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:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705};
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; Evidence={ECO:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719;
CC Evidence={ECO:0000305|PubMed:9371705};
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:0000250|UniProtKB:D3ZMY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715;
CC Evidence={ECO:0000250|UniProtKB:D3ZMY7};
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=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:0000250|UniProtKB:D3ZMY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380;
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:0000250|UniProtKB:D3ZMY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531;
CC Evidence={ECO:0000250|UniProtKB:D3ZMY7};
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:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705};
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:0000269|PubMed:8031149, ECO:0000269|PubMed:9371705};
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:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705};
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:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705};
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:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705};
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:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8031149};
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 (PubMed:9371705, PubMed:8031149).
CC Binding of an allosteric activator is a prerequisiste to magnesium and
CC substrate binding (By similarity). Inhibited by inorganic phosphate (By
CC similarity). {ECO:0000250|UniProtKB:P49902, ECO:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for IMP (in absence of allosteric activator)
CC {ECO:0000269|PubMed:8031149};
CC KM=0.09 mM for IMP (in the presence of 4.5 mM ATP)
CC {ECO:0000269|PubMed:8031149};
CC Vmax=12.5 umol/min/mg enzyme for the hydrolysis of IMP (in the
CC presence of 4.5 mM ATP) {ECO:0000269|PubMed:8031149};
CC Vmax=1.48 umol/min/mg enzyme for the hydrolysis of IMP (in absence of
CC the allosteric activator ATP) {ECO:0000269|PubMed:8031149};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8031149}.
CC -!- INTERACTION:
CC O46411; O46411: NT5C2; NbExp=3; IntAct=EBI-8487999, EBI-8487999;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8031149,
CC ECO:0000269|PubMed:9371705}.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000305}.
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DR EMBL; U73690; AAC48784.1; -; mRNA.
DR RefSeq; NP_776830.1; NM_174405.2.
DR RefSeq; XP_005225491.1; XM_005225434.3.
DR AlphaFoldDB; O46411; -.
DR SMR; O46411; -.
DR MINT; O46411; -.
DR STRING; 9913.ENSBTAP00000017090; -.
DR PaxDb; O46411; -.
DR PeptideAtlas; O46411; -.
DR PRIDE; O46411; -.
DR Ensembl; ENSBTAT00000068138; ENSBTAP00000071918; ENSBTAG00000012858.
DR GeneID; 281951; -.
DR KEGG; bta:281951; -.
DR CTD; 22978; -.
DR VEuPathDB; HostDB:ENSBTAG00000012858; -.
DR VGNC; VGNC:32291; NT5C2.
DR eggNOG; KOG2469; Eukaryota.
DR GeneTree; ENSGT00940000162369; -.
DR HOGENOM; CLU_017845_3_0_1; -.
DR InParanoid; O46411; -.
DR OrthoDB; 712212at2759; -.
DR TreeFam; TF315266; -.
DR BRENDA; 3.1.3.5; 908.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000012858; Expressed in thyroid gland and 107 other tissues.
DR ExpressionAtlas; O46411; baseline.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0050484; F:GMP 5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA: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; IDA:UniProtKB.
DR GO; GO:0046037; P:GMP metabolic process; IDA:UniProtKB.
DR GO; GO:0046040; P:IMP metabolic process; IDA:UniProtKB.
DR GO; GO:0046939; P:nucleotide phosphorylation; 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; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..560
FT /note="Cytosolic purine 5'-nucleotidase"
FT /id="PRO_0000310263"
FT REGION 541..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..560
FT /note="Required for tetramer assembly"
FT /evidence="ECO:0000250|UniProtKB:P49902"
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"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49902"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V1L4"
SQ SEQUENCE 560 AA; 64841 MW; 85E7CC64BF2581A0 CRC64;
MTTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTVCDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA
PQEITHCHDE DDDEEEEEEE
