ID   53DR_BPSPB              Reviewed;         172 AA.
AC   P68523; O31895; O64153;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=5'(3')-deoxyribonucleotidase {ECO:0000250|UniProtKB:P68522};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:P68522};
GN   Name=yorS; OrderedLocusNames=SPBc2p141;
OS   Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Spbetavirus.
OX   NCBI_TaxID=66797;
OH   NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10376821; DOI=10.1099/13500872-145-5-1055;
RA   Lazarevic V., Duesterhoeft A., Soldo B., Hilbert H., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the Bacillus subtilis temperate bacteriophage
RT   SPbetac2.";
RL   Microbiology 145:1055-1067(1999).
CC   -!- FUNCTION: Dephosphorylates nucleoside monophosphates such as the 5' and
CC       2'(3')-phosphates of deoxyribonucleotides in vitro. Also catalyzes the
CC       dephosphorylation of coenzyme A (CoA), pyridoxal-5'-phosphate (PLP),
CC       riboflavine-5-phosphate (FMN) and nicotinamide adenine dinucleotide
CC       phosphate (NADP) in vitro. {ECO:0000250|UniProtKB:P68522}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P68522};
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000305}.
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DR   EMBL; AF020713; AAC13113.1; -; Genomic_DNA.
DR   PIR; T12904; T12904.
DR   RefSeq; NP_046692.1; NC_001884.1.
DR   SMR; P68523; -.
DR   PRIDE; P68523; -.
DR   GeneID; 1261488; -.
DR   KEGG; vg:1261488; -.
DR   Proteomes; UP000009091; Genome.
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; Reference proteome.
FT   CHAIN           1..172
FT                   /note="5'(3')-deoxyribonucleotidase"
FT                   /id="PRO_0000164374"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
SQ   SEQUENCE   172 AA;  20417 MW;  CA89B7BA30226EE8 CRC64;
     MKKVIAIDMD QVLADLLSDW VAYINTYDDP FLKEKDILCW DIKKYTNTNN NVYRHLDYDL
     FRNLNVIEGS QRVTKELMKK YEVYVVTTAT NHPDSLKAKL EWLTEYFPFI PHSNVVLCGN
     KNIIKADIMI DDGIHNLESF EGMKILFDAP HNRNENRFIR VMNWEEIERK LL