DNPH1_DANRE
ID DNPH1_DANRE Reviewed; 143 AA.
AC B8A556;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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; ORFNames=si:ch211-117c8.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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; BX510320; CAX13259.1; -; Genomic_DNA.
DR RefSeq; NP_001156671.1; NM_001163199.1.
DR AlphaFoldDB; B8A556; -.
DR SMR; B8A556; -.
DR STRING; 7955.ENSDARP00000103969; -.
DR PaxDb; B8A556; -.
DR PeptideAtlas; B8A556; -.
DR Ensembl; ENSDART00000113060; ENSDARP00000103969; ENSDARG00000075730.
DR GeneID; 561810; -.
DR KEGG; dre:561810; -.
DR CTD; 10591; -.
DR ZFIN; ZDB-GENE-081107-5; dnph1.
DR eggNOG; ENOG502S2J2; Eukaryota.
DR GeneTree; ENSGT00390000001216; -.
DR HOGENOM; CLU_100069_1_0_1; -.
DR InParanoid; B8A556; -.
DR OMA; MHIYFCG; -.
DR OrthoDB; 1533988at2759; -.
DR PhylomeDB; B8A556; -.
DR TreeFam; TF329719; -.
DR Reactome; R-DRE-74259; Purine catabolism.
DR PRO; PR:B8A556; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000075730; Expressed in testis and 22 other tissues.
DR ExpressionAtlas; B8A556; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
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 Cytoplasm; Glycosidase; Hydrolase; Nucleotide metabolism; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..143
FT /note="2'-deoxynucleoside 5'-phosphate N-hydrolase 1"
FT /id="PRO_0000379457"
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:O43598"
FT BINDING 83
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 107..109
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 143 AA; 16186 MW; 477B90D245E1A61E CRC64;
MNIYFCGSIR GGRQDVVIYQ TIVKKLQQYG NVLTEHVSYD SLSDKGEDKD GDKAIHDRDV
QWLTMSDVIV AEVTQPSLGV GYELGRAVAM NKRILCLFRP FSGKVLSAMI RGASAKPLFQ
VQDYKEDEVE NILEEYFETL TKN
