ID   DNPH1_TETTS             Reviewed;         145 AA.
AC   Q24FH8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   ORFNames=TTHERM_00864850;
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210;
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG662285; EAS06480.1; -; Genomic_DNA.
DR   RefSeq; XP_001026725.1; XM_001026725.1.
DR   AlphaFoldDB; Q24FH8; -.
DR   SMR; Q24FH8; -.
DR   STRING; 5911.EAS06480; -.
DR   EnsemblProtists; EAS06480; EAS06480; TTHERM_00864850.
DR   GeneID; 7847114; -.
DR   KEGG; tet:TTHERM_00864850; -.
DR   eggNOG; ENOG502S2J2; Eukaryota.
DR   HOGENOM; CLU_100069_1_0_1; -.
DR   InParanoid; Q24FH8; -.
DR   OrthoDB; 1533988at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase; Nucleotide metabolism; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..145
FT                   /note="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase
FT                   1"
FT                   /id="PRO_0000379462"
FT   BINDING         9..15
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         24
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         41
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O35820"
FT   BINDING         88
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         113..115
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
SQ   SEQUENCE   145 AA;  16780 MW;  0D6F8660903E599F CRC64;
     MSQKKLTIYF CGSMRGVNAN HQNYQTIVQE LSKYGEVLTT HVAYPEMSNK LEHKMNDKQI
     YERDYSWFTE SQVMVAEVTA PSHGVGMELG WASLRQNYKT LCLSQKEKEF KTSGLIAGCP
     TFEYKEYQNQ EDIVAIIAEF MKQLQ