ID   DNPH1_METBF             Reviewed;         159 AA.
AC   Q46CC9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Mbar_A1510;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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   -!- 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; CP000099; AAZ70463.1; -; Genomic_DNA.
DR   RefSeq; WP_011306509.1; NC_007355.1.
DR   AlphaFoldDB; Q46CC9; -.
DR   SMR; Q46CC9; -.
DR   STRING; 269797.Mbar_A1510; -.
DR   EnsemblBacteria; AAZ70463; AAZ70463; Mbar_A1510.
DR   GeneID; 3626911; -.
DR   KEGG; mba:Mbar_A1510; -.
DR   eggNOG; arCOG02435; Archaea.
DR   HOGENOM; CLU_100069_1_0_2; -.
DR   OMA; MHIYFCG; -.
DR   OrthoDB; 112007at2157; -.
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.
FT   CHAIN           1..159
FT                   /note="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase
FT                   1"
FT                   /id="PRO_0000379467"
FT   BINDING         25..31
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         40
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         58
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O35820"
FT   BINDING         104
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         126..128
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
SQ   SEQUENCE   159 AA;  17848 MW;  47EA77C2A41C9120 CRC64;
     MKRLEKMEVS EKRIKVSEKR SPKIFLSGSI RGGRQLLGTY RFMFDTLEEA GAEVLSWHVA
     DPELEKTEMR MTEEEIYARD MGLLLKSDAL IAEVTVPSTG VGYEICRALV QRIPVLCLYS
     PDASVSAMVL GNPDHLLDAR AYPDKASLKK IITEFILAL