ID   53DR_STAAR              Reviewed;         180 AA.
AC   Q6GIR7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=SAR0778;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39788.1; -; Genomic_DNA.
DR   RefSeq; WP_000197262.1; NC_002952.2.
DR   AlphaFoldDB; Q6GIR7; -.
DR   SMR; Q6GIR7; -.
DR   KEGG; sar:SAR0778; -.
DR   HOGENOM; CLU_111510_0_0_9; -.
DR   OMA; FNAKFRW; -.
DR   OrthoDB; 1822108at2; -.
DR   Proteomes; UP000000596; 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_0000164383"
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;  20961 MW;  0C5BC1A658221275 CRC64;
     MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE
     PGFFRHLKVM PHAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF
     CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK