ID   53DR_STAAM              Reviewed;         180 AA.
AC   P66840; Q99VP8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=SAV0725;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB56887.1; -; Genomic_DNA.
DR   RefSeq; WP_000197262.1; NC_002758.2.
DR   AlphaFoldDB; P66840; -.
DR   SMR; P66840; -.
DR   World-2DPAGE; 0002:P66840; -.
DR   PaxDb; P66840; -.
DR   EnsemblBacteria; BAB56887; BAB56887; SAV0725.
DR   KEGG; sav:SAV0725; -.
DR   HOGENOM; CLU_111510_0_0_9; -.
DR   OMA; FNAKFRW; -.
DR   BioCyc; SAUR158878:SAV_RS03975-MON; -.
DR   Proteomes; UP000002481; 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_0000164381"
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