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5DNU_KLEP3
ID   5DNU_KLEP3              Reviewed;         199 AA.
AC   B5XNU9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=5'-deoxynucleotidase KPK_1466 {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=KPK_1466;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI11793.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XNU9; -.
DR   SMR; B5XNU9; -.
DR   EnsemblBacteria; ACI11793; ACI11793; KPK_1466.
DR   KEGG; kpe:KPK_1466; -.
DR   HOGENOM; CLU_084784_0_0_6; -.
DR   OMA; NQSHFFA; -.
DR   OrthoDB; 1508841at2; -.
DR   BioCyc; KPNE507522:GI0B-1466-MON; -.
DR   Proteomes; UP000001734; 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   CDD; cd00077; HDc; 1.
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 KPK_1466"
FT                   /id="PRO_1000136970"
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;  22711 MW;  8D03B18DCF1BC197 CRC64;
     MSQSHFFAHL SRLKLINRWP LMRNVRTENV SEHSLQVAMV AHALAAIKNR KFGGQVNAER
     IALLAMYHDA SEVLTGDLPT PVKYFNSQIA QEYKAIEKIA QQKLVDMVPD ELRDIFEPLI
     DEHHYSEEEQ SIVKQADALC AYLKCLEELS AGNNEFLLAK GRLEKTLASR RSAEMDYFMQ
     VFVPSFQLSL DEISQDSPL
 
 
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