5NT3_DANRE
ID 5NT3_DANRE Reviewed; 286 AA.
AC Q7SYN4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytosolic 5'-nucleotidase 3 {ECO:0000250|UniProtKB:Q9D020};
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9D020};
DE AltName: Full=Cytosolic 5'-nucleotidase III;
DE Short=cN-III;
GN Name=nt5c3; ORFNames=zgc:66117;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Can act both as nucleotidase and as phosphotransferase.
CC {ECO:0000250}.
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:0000250|UniProtKB:Q9D020};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54650.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC054650; AAH54650.1; ALT_INIT; mRNA.
DR RefSeq; NP_955854.1; NM_199560.1.
DR AlphaFoldDB; Q7SYN4; -.
DR SMR; Q7SYN4; -.
DR STRING; 7955.ENSDARP00000124389; -.
DR PaxDb; Q7SYN4; -.
DR PeptideAtlas; Q7SYN4; -.
DR PRIDE; Q7SYN4; -.
DR GeneID; 321720; -.
DR KEGG; dre:321720; -.
DR CTD; 51251; -.
DR ZFIN; ZDB-GENE-030131-439; nt5c3a.
DR eggNOG; KOG3128; Eukaryota.
DR InParanoid; Q7SYN4; -.
DR OrthoDB; 1171042at2759; -.
DR PhylomeDB; Q7SYN4; -.
DR Reactome; R-DRE-73621; Pyrimidine catabolism.
DR PRO; PR:Q7SYN4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07504; HAD_5NT; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR Pfam; PF05822; UMPH-1; 1.
DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01544; HAD-SF-IE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Cytosolic 5'-nucleotidase 3"
FT /id="PRO_0000328952"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
SQ SEQUENCE 286 AA; 32937 MW; D738506E6B9DC4DF CRC64;
MMPEFEKNTV HIRDPERVEQ IICGLIKGGA SKLQIITDFD MTLSRFAVNG KRCPSCHNII
DNSKLVTDDC RKKLVHLKET YYPIEIDPHL TMEEKYPFMV EWYFKSHTLL VEQRLEKDKL
PEAVRESDVS LKEGYEQFFD RLHQHSVPVF IFSAGLGDVL EEIIRQAGVY HPNVKVVSNF
MDFDDNGVLK GFKGELIHVY NKHDGALRNT EYFKQLKDNG NIILLGDSLG DLTMADGVPN
VENILKIGYL NDKVEELLEK YMDSYNIVLA RDETLEVPNS ILQKIL
