ID   53DR_BORPE              Reviewed;         186 AA.
AC   Q7W066;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=BP0294;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640411; CAE40672.1; -; Genomic_DNA.
DR   RefSeq; NP_879172.1; NC_002929.2.
DR   RefSeq; WP_004566083.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7W066; -.
DR   SMR; Q7W066; -.
DR   STRING; 257313.BP0294; -.
DR   GeneID; 45387745; -.
DR   KEGG; bpe:BP0294; -.
DR   PATRIC; fig|257313.5.peg.317; -.
DR   eggNOG; COG4502; Bacteria.
DR   HOGENOM; CLU_100259_0_0_4; -.
DR   OMA; YAWIEKH; -.
DR   Proteomes; UP000002676; 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; Reference proteome.
FT   CHAIN           1..186
FT                   /note="Putative 5'(3')-deoxyribonucleotidase"
FT                   /id="PRO_0000164377"
FT   ACT_SITE        6
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        8
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305"
FT   BINDING         6
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
SQ   SEQUENCE   186 AA;  21679 MW;  9073B436FBD9FD28 CRC64;
     MLILLDQDGV LADFEHAFID AWRKRHPDIE PVAFEERKSF HIREDYAPEL RGLAEAIYTA
     PGFIRDLPPV PGAVEAFREL LALGMDVRIC SSPLMQFENC VAEKYLWVER HLGRDATQRL
     ILTRDKTLVQ GDLLIDDRPV ITGAARPRWR HIIYDAPYNR DQTDRPRLDW RNWRNVLAGE
     LYRSDA