53DR_STAEQ
ID 53DR_STAEQ Reviewed; 179 AA.
AC Q5HR07;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE EC=3.1.3.-;
GN OrderedLocusNames=SERP0388;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53769.1; -; Genomic_DNA.
DR RefSeq; WP_001832599.1; NC_002976.3.
DR AlphaFoldDB; Q5HR07; -.
DR SMR; Q5HR07; -.
DR EnsemblBacteria; AAW53769; AAW53769; SERP0388.
DR GeneID; 50019347; -.
DR KEGG; ser:SERP0388; -.
DR eggNOG; COG4502; Bacteria.
DR HOGENOM; CLU_111510_0_0_9; -.
DR OMA; FNAKFRW; -.
DR OrthoDB; 1822108at2; -.
DR Proteomes; UP000000531; 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..179
FT /note="Putative 5'(3')-deoxyribonucleotidase"
FT /id="PRO_0000164387"
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 179 AA; 20944 MW; ED5BA6437DE442DD CRC64;
MTRQRIAIDM DEVLADTLGA VVKAVNERAD LNIKMESLNG KKLKHMIPEH EGLVMDILKE
PGFFRNLDVM PHAQEVVKQL NEHYDIYIAT AAMDVPTSFH DKYEWLLEYF PFLDPQHFVF
CGRKNIILAD YLIDDNPKQL EIFEGKSIMF TASHNVNEHR FERVSGWRDV KNYFNSIEK