ID 5N3BB_XENLA Reviewed; 290 AA. AC Q2TAG6; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 02-SEP-2026, entry version 85. DE RecName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase B {ECO:0000250|UniProtKB:Q9W197}; DE Short=7-methylguanosine nucleotidase B; DE EC=3.1.3.91 {ECO:0000250|UniProtKB:Q9W197}; DE AltName: Full=Cytosolic 5'-nucleotidase 3B-B; DE AltName: Full=Cytosolic 5'-nucleotidase III-like protein B {ECO:0000250|UniProtKB:Q9W197}; DE Short=cN-III-like protein B; DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9W197}; DE AltName: Full=N(7)-methylguanylate 5'-phosphatase B; GN Name=Nt5c3b-b; Synonyms=Nt5c3l-b; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Oocyte; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate CC (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific CC activity for m(7)GMP may protect cells against undesired salvage of CC m(7)GMP and its incorporation into nucleic acids. Also has weak CC activity for CMP. UMP and purine nucleotides are poor substrates (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(7)-methyl-GMP + H2O = N(7)-methylguanosine + phosphate; CC Xref=Rhea:RHEA:37107, ChEBI:CHEBI:15377, ChEBI:CHEBI:20794, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58285; EC=3.1.3.91; CC Evidence={ECO:0000250|UniProtKB:Q9W197}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CMP + H2O = cytidine + phosphate; Xref=Rhea:RHEA:29367, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17562, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:60377; EC=3.1.3.91; CC Evidence={ECO:0000250|UniProtKB:Q9W197}; 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:Q9W197}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC110937; AAI10938.1; -; mRNA. DR RefSeq; NP_001082544.1; NM_001089075.1. DR AlphaFoldDB; Q2TAG6; -. DR SMR; Q2TAG6; -. DR DNASU; 398553; -. DR GeneID; 398553; -. DR KEGG; xla:398553; -. DR AGR; Xenbase:XB-GENE-992511; -. DR CTD; 398553; -. DR OrthoDB; 10014216at2759; -. DR Proteomes; UP000186698; Chromosome 9_10L. DR Bgee; 398553; Expressed in liver and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR CDD; cd07504; HAD_5NT; 1. DR FunFam; 1.10.150.340:FF:000001; Cytosolic 5-nucleotidase 3-like; 1. DR FunFam; 3.40.50.1000:FF:000032; Cytosolic 5-nucleotidase 3-like; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu. DR NCBIfam; TIGR01544; HAD-SF-IE; 1. DR PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1. DR PANTHER; PTHR13045:SF15; 7-METHYLGUANOSINE PHOSPHATE-SPECIFIC 5'-NUCLEOTIDASE; 1. DR Pfam; PF05822; UMPH-1; 1. DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..290 FT /note="7-methylguanosine phosphate-specific 5'-nucleotidase FT B" FT /id="PRO_0000328954" FT ACT_SITE 39 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q9W197" FT ACT_SITE 41 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q9W197" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9W197" FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9W197" FT BINDING 86 FT /ligand="CMP" FT /ligand_id="ChEBI:CHEBI:60377" FT /evidence="ECO:0000250|UniProtKB:Q9W197" FT BINDING 86 FT /ligand="N(7)-methyl-GMP" FT /ligand_id="ChEBI:CHEBI:58285" FT /evidence="ECO:0000250|UniProtKB:Q9W197" FT BINDING 154..155 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9H0P0" FT BINDING 203 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9D020" FT BINDING 228 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9W197" SQ SEQUENCE 290 AA; 33537 MW; F0E2954238E8041D CRC64; MRLPVLGKDT VRMRDPEGLQ DKITRIQRGG QEKLQIISDF DMTLSRFSRN GERCPTCYNI IDNSNIISDE GRKKLKCLFD IYYPLEIDPK KSIEEKYPLM VEWWSKAHDL FYEQRIQKDR LAQVVKEPQA TLRDGYDLFF NNLYQREIPL FIFSAGIGDV LEEIIRQAGV FHPNTKVVSN YMDFDDNGIL TGFKGDLIHT YNKNSSVLKD TEYFKEISHR TNILLLGDTL GDLTMADGVS TVENIIKIGF LNDKVEELTE QFLQSYDIVL LRDETLDVVN GILQFVTAKN //