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Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (Cytosolic 5'-nucleotidase II) (Cytosolic IMP/GMP-specific 5'-nucleotidase)

 5NTC_BOVIN              Reviewed;         560 AA.
O46411;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 108.
RecName: Full=Cytosolic purine 5'-nucleotidase;
EC=3.1.3.5;
AltName: Full=Cytosolic 5'-nucleotidase II;
AltName: Full=Cytosolic IMP/GMP-specific 5'-nucleotidase;
Name=NT5C2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Thymus;
PubMed=9371705; DOI=10.1042/bj3280483;
Allegrini S., Pesi R., Tozzi M.G., Fiol C.J., Johnson R.B.,
Eriksson S.;
"Bovine cytosolic IMP/GMP-specific 5'-nucleotidase: cloning and
expression of active enzyme in Escherichia coli.";
Biochem. J. 328:483-487(1997).
-!- FUNCTION: May have a critical role in the maintenance of a
constant composition of intracellular purine/pyrimidine
nucleotides in cooperation with other nucleotidases.
Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other
purine nucleotides. {ECO:0000269|PubMed:9371705}.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Allosterically activated by various
compounds, including ATP. {ECO:0000250}.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-8487999, EBI-8487999;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
{ECO:0000305}.
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EMBL; U73690; AAC48784.1; -; mRNA.
RefSeq; NP_776830.1; NM_174405.2.
RefSeq; XP_005225491.1; XM_005225434.3.
UniGene; Bt.5382; -.
ProteinModelPortal; O46411; -.
SMR; O46411; -.
MINT; O46411; -.
STRING; 9913.ENSBTAP00000017090; -.
PaxDb; O46411; -.
PeptideAtlas; O46411; -.
PRIDE; O46411; -.
Ensembl; ENSBTAT00000017090; ENSBTAP00000017090; ENSBTAG00000012858.
GeneID; 281951; -.
KEGG; bta:281951; -.
CTD; 22978; -.
VGNC; VGNC:32291; NT5C2.
eggNOG; KOG2469; Eukaryota.
eggNOG; ENOG410XQAV; LUCA.
GeneTree; ENSGT00550000074539; -.
HOGENOM; HOG000246075; -.
HOVERGEN; HBG000025; -.
InParanoid; O46411; -.
KO; K01081; -.
OMA; ACLYTSR; -.
OrthoDB; EOG091G074N; -.
TreeFam; TF315266; -.
BRENDA; 3.1.3.5; 908.
Reactome; R-BTA-2161541; Abacavir metabolism.
Reactome; R-BTA-74259; Purine catabolism.
Proteomes; UP000009136; Chromosome 26.
Bgee; ENSBTAG00000012858; Expressed in 9 organ(s), highest expression level in prefrontal cortex.
ExpressionAtlas; O46411; baseline and differential.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0046085; P:adenosine metabolic process; IBA:GO_Central.
GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
InterPro; IPR023214; HAD_sf.
InterPro; IPR016695; Pur_nucleotidase.
PANTHER; PTHR12103; PTHR12103; 1.
Pfam; PF05761; 5_nucleotid; 1.
PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
1: Evidence at protein level;
Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase; Magnesium;
Metal-binding; Nucleotide metabolism; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 560 Cytosolic purine 5'-nucleotidase.
/FTId=PRO_0000310263.
REGION 202 210 Substrate binding. {ECO:0000255}.
COMPBIAS 549 560 Asp/Glu-rich (acidic).
ACT_SITE 52 52 Nucleophile. {ECO:0000250}.
ACT_SITE 54 54 Proton donor. {ECO:0000250}.
METAL 52 52 Magnesium. {ECO:0000250}.
METAL 54 54 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 351 351 Magnesium. {ECO:0000250}.
BINDING 127 127 Allosteric activator 1. {ECO:0000250}.
BINDING 154 154 Allosteric activator 2. {ECO:0000250}.
BINDING 354 354 Allosteric activator 2. {ECO:0000250}.
BINDING 436 436 Allosteric activator 1; via carbonyl
oxygen. {ECO:0000250}.
BINDING 453 453 Allosteric activator 2. {ECO:0000250}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000250|UniProtKB:P49902}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:P49902}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000250|UniProtKB:P49902}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000250|UniProtKB:Q3V1L4}.
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


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