ID   5DNU_VIBVU              Reviewed;         179 AA.
AC   Q8DG35;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=5'-deoxynucleotidase VV1_0013 {ECO:0000255|HAMAP-Rule:MF_01100};
DE            EC=3.1.3.89 {ECO:0000255|HAMAP-Rule:MF_01100};
DE   AltName: Full=5'-deoxyribonucleotidase {ECO:0000255|HAMAP-Rule:MF_01100};
DE   AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01100};
GN   OrderedLocusNames=VV1_0013;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'-
CC       deoxyribonucleoside 5'-monophosphates. {ECO:0000255|HAMAP-
CC       Rule:MF_01100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC         deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:65317; EC=3.1.3.89; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01100};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01100};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01100}.
CC   -!- SIMILARITY: Belongs to the 5DNU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01100}.
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DR   EMBL; AE016795; AAO08557.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8DG35; -.
DR   SMR; Q8DG35; -.
DR   EnsemblBacteria; AAO08557; AAO08557; VV1_0013.
DR   KEGG; vvu:VV1_0013; -.
DR   HOGENOM; CLU_1502898_0_0_6; -.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01100; 5DNU; 1.
DR   InterPro; IPR022971; YfbR.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..179
FT                   /note="5'-deoxynucleotidase VV1_0013"
FT                   /id="PRO_0000095063"
FT   BINDING         53
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         62..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         122
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
SQ   SEQUENCE   179 AA;  20714 MW;  98DDA302B31DEE7E CRC64;
     MLQTTLKYRN RCNICVREYK CCIGSFMSRF GLSNMALTHY LTSIIHSFTS LAHQMLKRTN
     QDLPTPVKYY NPEIAKEYKK IEAAAEQKLL SMLPEEFQED FRPFVISQQT SEEEAQIVKQ
     ADSICAYLKC LEELSAGNHE FALAKKRLDI TLAERKTPEM DYFLNTFAPS FELSLDEIS