ID   DNPH1_ESOLU             Reviewed;         145 AA.
AC   C1BW56;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=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   Name=dnph1;
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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. Deoxyribonucleoside 5'-monophosphates
CC       containing purine bases are preferred to those containing pyrimidine
CC       bases. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03036}.
CC       Nucleus {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; BT078835; ACO13259.1; -; mRNA.
DR   RefSeq; NP_001291112.1; NM_001304183.1.
DR   AlphaFoldDB; C1BW56; -.
DR   SMR; C1BW56; -.
DR   STRING; 8010.XP_010894530.1; -.
DR   Ensembl; ENSELUT00000040065; ENSELUP00000017175; ENSELUG00000016938.
DR   GeneID; 105025506; -.
DR   KEGG; els:105025506; -.
DR   CTD; 10591; -.
DR   GeneTree; ENSGT00390000001216; -.
DR   OMA; MHIYFCG; -.
DR   OrthoDB; 1533988at2759; -.
DR   Proteomes; UP000265140; LG06.
DR   Bgee; ENSELUG00000016938; Expressed in embryo and 11 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070694; F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity; IEA:InterPro.
DR   GO; GO:0009159; P:deoxyribonucleoside monophosphate catabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycosidase; Hydrolase; Nucleotide metabolism; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..145
FT                   /note="2'-deoxynucleoside 5'-phosphate N-hydrolase 1"
FT                   /id="PRO_0000379458"
FT   BINDING         4..10
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         19
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         36
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O35820"
FT   BINDING         85
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         109..111
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   145 AA;  16378 MW;  435AC28908D80685 CRC64;
     MHIYFCGSIR GGRQDVIIYQ RIVQTLQKYG EVLTEHVSHS DLSERGEDAV QDGDKFIHDR
     DMEWLVMSDV IIAEVTQPSL GVGYELGSAR GMRKKILCLF RPSSGKSLSA MVRGAVDGSL
     FQVRDYKEEE VEGILEEYFK GLSKD