ID   53DR_CLOAB              Reviewed;         180 AA.
AC   Q97JQ5;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=5'(3')-deoxyribonucleotidase {ECO:0000305|PubMed:25848029};
DE            EC=3.1.3.- {ECO:0000305|PubMed:25848029};
GN   OrderedLocusNames=CA_C1218;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
RN   [2]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA   Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA   Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA   Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA   Allen K.N., Farelli J.D.;
RT   "Panoramic view of a superfamily of phosphatases through substrate
RT   profiling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC   -!- FUNCTION: Dephosphorylates nucleoside monophosphates such as the 5' and
CC       2'(3')-phosphates of deoxyribonucleotides in vitro.
CC       {ECO:0000269|PubMed:25848029}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25848029};
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000305}.
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DR   EMBL; AE001437; AAK79190.1; -; Genomic_DNA.
DR   PIR; C97050; C97050.
DR   RefSeq; NP_347850.1; NC_003030.1.
DR   RefSeq; WP_010964531.1; NC_003030.1.
DR   AlphaFoldDB; Q97JQ5; -.
DR   SMR; Q97JQ5; -.
DR   STRING; 272562.CA_C1218; -.
DR   DNASU; 1117401; -.
DR   EnsemblBacteria; AAK79190; AAK79190; CA_C1218.
DR   GeneID; 44997725; -.
DR   KEGG; cac:CA_C1218; -.
DR   PATRIC; fig|272562.8.peg.1420; -.
DR   eggNOG; COG4502; Bacteria.
DR   HOGENOM; CLU_111510_0_0_9; -.
DR   OMA; FNAKFRW; -.
DR   OrthoDB; 1822108at2; -.
DR   Proteomes; UP000000814; 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..180
FT                   /note="5'(3')-deoxyribonucleotidase"
FT                   /id="PRO_0000164378"
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         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CTG7"
SQ   SEQUENCE   180 AA;  21274 MW;  1AC58D7A55370CF8 CRC64;
     MNKPTLGIDL DTTLNTLDRE WVKRYNEIYK DKLLPSDIKG WDIENYVKPE CGKKIYDILK
     EPHFFRNLGV QPFAETALEE LTSIFNIYIV SATHYKVCED KGNWIKEKFP FISYQNIIFC
     HNKGLVHLDI LIDDNPLNLE NFKGNKILFD AHHNKSENRF VRARDWYEAK ALCESLKDFL