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5DNU_PECCP
ID   5DNU_PECCP              Reviewed;         199 AA.
AC   C6DA49;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=5'-deoxynucleotidase PC1_2775 {ECO:0000255|HAMAP-Rule:MF_01100};
DE            EC=3.1.3.89 {ECO:0000255|HAMAP-Rule:MF_01100};
DE   AltName: Full=5'-deoxyribonucleotidase {ECO:0000255|HAMAP-Rule:MF_01100};
DE   AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01100};
GN   OrderedLocusNames=PC1_2775;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'-
CC       deoxyribonucleoside 5'-monophosphates. {ECO:0000255|HAMAP-
CC       Rule:MF_01100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC         deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:65317; EC=3.1.3.89; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01100};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01100};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01100}.
CC   -!- SIMILARITY: Belongs to the 5DNU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01100}.
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DR   EMBL; CP001657; ACT13805.1; -; Genomic_DNA.
DR   RefSeq; WP_015840969.1; NC_012917.1.
DR   AlphaFoldDB; C6DA49; -.
DR   SMR; C6DA49; -.
DR   STRING; 561230.PC1_2775; -.
DR   EnsemblBacteria; ACT13805; ACT13805; PC1_2775.
DR   KEGG; pct:PC1_2775; -.
DR   eggNOG; COG1896; Bacteria.
DR   HOGENOM; CLU_084784_0_0_6; -.
DR   OMA; NQSHFFA; -.
DR   OrthoDB; 1508841at2; -.
DR   Proteomes; UP000002736; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002953; F:5'-deoxynucleotidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01100; 5DNU; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR022971; YfbR.
DR   InterPro; IPR039356; YfbR/HDDC2.
DR   PANTHER; PTHR11845; PTHR11845; 1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..199
FT                   /note="5'-deoxynucleotidase PC1_2775"
FT                   /id="PRO_1000213544"
FT   DOMAIN          30..142
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   BINDING         18..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         33
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         68
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         69
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         77..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
FT   SITE            18
FT                   /note="Appears to be important in orienting the phosphate
FT                   for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01100"
SQ   SEQUENCE   199 AA;  22924 MW;  5DD5D582416657DF CRC64;
     MNQSHFFAHL SRLKLISRWP LMRNVRTENV SEHSLQVAFV AHALAVIKNR KFEGNLNAER
     IALLAMYHDA SEVLTGDMPT PIKYYNAQIA HEYKKIEKIA QQKLVEMLPE ELQQDYRMLL
     DDSYTSEEER AIVKQADALC AYLKCLEELS AGNAEFTLAK ARLEKTLQLR HSPEMDYFMT
     VFVPSFSLSL DEISQDSPL
 
 
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