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5'-deoxynucleotidase CSK29544_02236 (EC 3.1.3.89) (5'-deoxyribonucleotidase) (Nucleoside 5'-monophosphate phosphohydrolase)

 A0A0F6SBB3_CROSK        Unreviewed;       199 AA.
A0A0F6SBB3;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
25-OCT-2017, entry version 20.
RecName: Full=5'-deoxynucleotidase CSK29544_02236 {ECO:0000256|HAMAP-Rule:MF_01100};
EC=3.1.3.89 {ECO:0000256|HAMAP-Rule:MF_01100};
AltName: Full=5'-deoxyribonucleotidase {ECO:0000256|HAMAP-Rule:MF_01100};
AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_01100};
ORFNames=CSK29544_02236 {ECO:0000313|EMBL:AKE95193.1};
Cronobacter sakazakii (Enterobacter sakazakii).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Cronobacter.
NCBI_TaxID=28141 {ECO:0000313|EMBL:AKE95193.1, ECO:0000313|Proteomes:UP000034520};
[1] {ECO:0000313|EMBL:AKE95193.1, ECO:0000313|Proteomes:UP000034520}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29544 {ECO:0000313|EMBL:AKE95193.1,
ECO:0000313|Proteomes:UP000034520};
Kim S., Ryu S., Choi S., Lee J.-H.;
Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'-
deoxyribonucleoside 5'-monophosphates. {ECO:0000256|HAMAP-
Rule:MF_01100, ECO:0000256|SAAS:SAAS00805799}.
-!- CATALYTIC ACTIVITY: A 2'-deoxyribonucleoside 5'-monophosphate +
H(2)O = a 2'-deoxyribonucleoside + phosphate. {ECO:0000256|HAMAP-
Rule:MF_01100, ECO:0000256|SAAS:SAAS00805800}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000256|HAMAP-Rule:MF_01100};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01100,
ECO:0000256|SAAS:SAAS00805801}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01100,
ECO:0000256|SAAS:SAAS00805804}.
-!- SIMILARITY: Belongs to the 5DNU family. {ECO:0000256|HAMAP-
Rule:MF_01100, ECO:0000256|SAAS:SAAS00805803}.
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EMBL; CP011047; AKE95193.1; -; Genomic_DNA.
RefSeq; WP_007699992.1; NZ_NHTW01000001.1.
ProteinModelPortal; A0A0F6SBB3; -.
SMR; A0A0F6SBB3; -.
EnsemblBacteria; AKE95193; AKE95193; CSK29544_02236.
GeneID; 29458013; -.
KEGG; csj:CSK29544_02236; -.
PATRIC; fig|28141.62.peg.923; -.
KO; K08722; -.
Proteomes; UP000034520; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
CDD; cd00077; HDc; 1.
HAMAP; MF_01100; 5DNU; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR022971; YfbR.
Pfam; PF13023; HD_3; 1.
SMART; SM00471; HDc; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000034520};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01100,
ECO:0000256|SAAS:SAAS00805806};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01100,
ECO:0000256|SAAS:SAAS00805796};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01100,
ECO:0000256|SAAS:SAAS00805798};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01100,
ECO:0000256|SAAS:SAAS00805805}.
DOMAIN 26 151 HDc. {ECO:0000259|SMART:SM00471}.
REGION 18 19 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01100}.
REGION 77 80 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01100}.
METAL 33 33 Divalent metal cation; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01100}.
METAL 68 68 Divalent metal cation; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01100}.
METAL 69 69 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01100}.
METAL 137 137 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01100}.
BINDING 33 33 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01100}.
BINDING 69 69 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01100}.
BINDING 137 137 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01100}.
SITE 18 18 Appears to be important in orienting the
phosphate for catalysis.
{ECO:0000256|HAMAP-Rule:MF_01100}.
SEQUENCE 199 AA; 22816 MW; 5234F42B60756970 CRC64;
MSQSHFFAYL SRLKLINRWP LMRNVRTENV SEHSLQVAMV AHALAVIKNR KFQGNVNPER
IALLAMYHDA SEVLTGDLPT PVKYFNSQIA HEYKAIEKIA QQKLIAMVPE ELQDIFAPLL
DEHHYTEDEK SLVKQADALC AYLKCLEELS AGNNEFLLAK SRLEKTLAQR HSAEMDYFMQ
VFVPSFHLSL DEISQDSPL


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