5N3BB_XENLA
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 03-AUG-2022, entry version 76.
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=H2O + N(7)-methyl-GMP = 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}.
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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 CTD; 398553; -.
DR OrthoDB; 1171042at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 398553; Expressed in liver and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; 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.
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
