ID   DNPH1_THEPD             Reviewed;         143 AA.
AC   A1RW47;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036};
DE            EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};
GN   OrderedLocusNames=Tpen_0017;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
CC   -!- FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of
CC       deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate
CC       and a purine or pyrimidine base. {ECO:0000255|HAMAP-Rule:MF_03036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-
CC         deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase;
CC         Xref=Rhea:RHEA:57852, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432,
CC         ChEBI:CHEBI:62877, ChEBI:CHEBI:142209; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03036};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-
CC         D-ribose 5-phosphate + a purine nucleobase; Xref=Rhea:RHEA:51132,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:26386, ChEBI:CHEBI:62877,
CC         ChEBI:CHEBI:142198; Evidence={ECO:0000255|HAMAP-Rule:MF_03036};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_03036}.
CC   -!- SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase
CC       1 family. {ECO:0000255|HAMAP-Rule:MF_03036}.
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DR   EMBL; CP000505; ABL77427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1RW47; -.
DR   SMR; A1RW47; -.
DR   STRING; 368408.Tpen_0017; -.
DR   EnsemblBacteria; ABL77427; ABL77427; Tpen_0017.
DR   KEGG; tpe:Tpen_0017; -.
DR   eggNOG; arCOG02435; Archaea.
DR   HOGENOM; CLU_100069_1_0_2; -.
DR   OMA; MHIYFCG; -.
DR   OrthoDB; 112007at2157; -.
DR   Proteomes; UP000000641; Chromosome.
DR   GO; GO:0070694; F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity; ISS:UniProtKB.
DR   GO; GO:0009159; P:deoxyribonucleoside monophosphate catabolic process; ISS:UniProtKB.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_03036; Nuc_phosphate_hydrolase; 1.
DR   InterPro; IPR028607; DNPH1.
DR   InterPro; IPR007710; Nucleoside_deoxyribTrfase.
DR   Pfam; PF05014; Nuc_deoxyrib_tr; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..143
FT                   /note="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase
FT                   1"
FT                   /id="PRO_0000379469"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O35820"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT   BINDING         106..108
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
SQ   SEQUENCE   143 AA;  16043 MW;  7C484EE6309BC0CB CRC64;
     MKVYLAAPMR GDRSALANVK KLLQALEERG YVVLTKHVAD DVLDVEKGMT PREVFERDIR
     LLEEADVLVA EVSYPSLGVG FEIAYFLLRG KPVIALALRE RLESVSAMIR GITWENFRLV
     AYSDVDEAIE KLDSMLPGSV DMQ