ID   53DR_STAAW              Reviewed;         180 AA.
AC   Q8NXN2;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=MW0687;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of
CC       deoxyribonucleotides. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q97JQ5};
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB94552.1; -; Genomic_DNA.
DR   RefSeq; WP_000197271.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXN2; -.
DR   SMR; Q8NXN2; -.
DR   EnsemblBacteria; BAB94552; BAB94552; BAB94552.
DR   KEGG; sam:MW0687; -.
DR   HOGENOM; CLU_111510_0_0_9; -.
DR   OMA; FNAKFRW; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR010708; 5'(3')-deoxyribonucleotidase.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF06941; NT5C; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..180
FT                   /note="Putative 5'(3')-deoxyribonucleotidase"
FT                   /id="PRO_0000164385"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        11
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
SQ   SEQUENCE   180 AA;  20987 MW;  11ED077D3C734330 CRC64;
     MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE
     PGFFRHLKVM PYAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF
     CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK