ID   5N3BA_XENLA             Reviewed;         290 AA.
AC   Q7ZWS2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase A {ECO:0000250|UniProtKB:Q9H0P0};
DE            Short=7-methylguanosine nucleotidase A;
DE            EC=3.1.3.91 {ECO:0000250|UniProtKB:Q9H0P0};
DE   AltName: Full=Cytosolic 5'-nucleotidase 3B-A;
DE   AltName: Full=Cytosolic 5'-nucleotidase III-like protein A {ECO:0000250|UniProtKB:Q9H0P0};
DE            Short=cN-III-like protein A;
DE            EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9H0P0};
DE   AltName: Full=N(7)-methylguanylate 5'-phosphatase A;
GN   Name=Nt5c3b-a; Synonyms=Nt5c3l-a;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) 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:Q9H0P0};
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:Q9H0P0};
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:Q9H0P0};
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; BC046729; AAH46729.2; -; mRNA.
DR   AlphaFoldDB; Q7ZWS2; -.
DR   SMR; Q7ZWS2; -.
DR   MaxQB; Q7ZWS2; -.
DR   OMA; EIDPYRT; -.
DR   Proteomes; UP000186698; Genome assembly.
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                   A"
FT                   /id="PRO_0000328953"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT   ACT_SITE        41
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0P0"
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:Q9H0P0"
SQ   SEQUENCE   290 AA;  33500 MW;  DE1147A21EF1C317 CRC64;
     MRLPVLGKDT VRMRDPEGLQ DKITRIQRGG QEKLQIISDF DMTLSRFSRN GERCPTCYNI
     IDNSNIISDE GRKKLKCLFD IYYPLEIDPK KSIEEKYPLM VEWWSKAHDL FYEQRIQKDR
     LAQVVKESQA TLRDGYDLFF NSLYQREIPL FIFSAGIGDV LEEIIRQAGV FHPNTKVVSN
     YMDFDDNGIL TGFKGDLIHT YNKNSSVLKD TEYFKEISHR TNILLLGDTL GDLTMADGVS
     TVENIIKIGF LNDKVEELTE QFLQSYDIVL LRDETLDVVN GILQFVTAKN