DNPH1_TETNG
ID DNPH1_TETNG Reviewed; 142 AA.
AC Q4S2L4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 59.
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=GSTENG00025030001;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG05118.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CAAE01014760; CAG05118.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q4S2L4; -.
DR SMR; Q4S2L4; -.
DR STRING; 99883.ENSTNIP00000016373; -.
DR KEGG; tng:GSTEN00025030G001; -.
DR InParanoid; Q4S2L4; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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..142
FT /note="2'-deoxynucleoside 5'-phosphate N-hydrolase 1"
FT /id="PRO_0000379459"
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 84
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 108..110
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 142 AA; 16130 MW; 59321F9D1959C310 CRC64;
MKVYFCGSIR GGRDDAELYH RMVAKLQSFA TVLTEHVGRR ELGDTGEHVT QGDRFIHDRD
VDWLRQSDVV VAEVTQPSLG VGYELGRAVD MKKKVLCLFR PSSGRRLSAM IRGADNGDSF
VVRDYCQDEI EQVLEDFFSN QK
