DNPH1_SYNC1
ID DNPH1_SYNC1 Reviewed; 142 AA.
AC Q3A6G9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Pcar_0779;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000142; ABA88038.1; -; Genomic_DNA.
DR RefSeq; WP_011340487.1; NC_007498.2.
DR AlphaFoldDB; Q3A6G9; -.
DR SMR; Q3A6G9; -.
DR STRING; 338963.Pcar_0779; -.
DR EnsemblBacteria; ABA88038; ABA88038; Pcar_0779.
DR KEGG; pca:Pcar_0779; -.
DR eggNOG; COG3613; Bacteria.
DR HOGENOM; CLU_100069_1_0_7; -.
DR OMA; MHIYFCG; -.
DR OrthoDB; 1838260at2; -.
DR Proteomes; UP000002534; Chromosome.
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; Reference proteome.
FT CHAIN 1..142
FT /note="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase
FT 1"
FT /id="PRO_0000379464"
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 82
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 106..108
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
SQ SEQUENCE 142 AA; 15745 MW; 3598F7F72A6FAA50 CRC64;
MKIFFSGSIR GGNKYRRQYG QILAFLQAFG ETISEHSDRP EAFDDGGLKG DAAIYARDTH
WIREADLLVA EVSQPSIGVG YEIAYAEARN IPILALYHVG AESPMSAMVF GNPKITSIRY
DSLSELWPVL KDTLAETHLP PK
