53DR_STAAN
ID 53DR_STAAN Reviewed; 180 AA.
AC P66841; Q99VP8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE EC=3.1.3.-;
GN OrderedLocusNames=SA0680;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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; BA000018; BAB41913.1; -; Genomic_DNA.
DR PIR; F89844; F89844.
DR RefSeq; WP_000197262.1; NC_002745.2.
DR AlphaFoldDB; P66841; -.
DR SMR; P66841; -.
DR EnsemblBacteria; BAB41913; BAB41913; BAB41913.
DR KEGG; sau:SA0680; -.
DR HOGENOM; CLU_111510_0_0_9; -.
DR OMA; FNAKFRW; -.
DR Proteomes; UP000000751; 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_0000164382"
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