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SURE_YERPS
ID   SURE_YERPS              Reviewed;         254 AA.
AC   Q66EC0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=5'/3'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.6 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Exopolyphosphatase {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.6.1.11 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Nucleoside monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060};
GN   Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; OrderedLocusNames=YPTB0773;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Nucleotidase with a broad substrate specificity as it can
CC       dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates
CC       and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP.
CC       Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the
CC       preference for short-chain-length substrates (P20-25). Might be
CC       involved in the regulation of dNTP and NTP pools, and in the turnover
CC       of 3'-mononucleotides produced by numerous intracellular RNases (T1,
CC       T2, and F) during the degradation of various RNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_00060}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC         ChEBI:CHEBI:43474; EC=3.6.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00060};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00060};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}.
CC   -!- SIMILARITY: Belongs to the SurE nucleotidase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00060}.
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DR   EMBL; BX936398; CAH20013.1; -; Genomic_DNA.
DR   RefSeq; WP_011191778.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66EC0; -.
DR   SMR; Q66EC0; -.
DR   EnsemblBacteria; CAH20013; CAH20013; YPTB0773.
DR   GeneID; 66842806; -.
DR   KEGG; ypo:BZ17_1783; -.
DR   KEGG; yps:YPTB0773; -.
DR   PATRIC; fig|273123.14.peg.1888; -.
DR   OMA; DCVHIAL; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1210.10; -; 1.
DR   HAMAP; MF_00060; SurE; 1.
DR   InterPro; IPR030048; SurE.
DR   InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR   InterPro; IPR036523; SurE-like_sf.
DR   PANTHER; PTHR30457; PTHR30457; 1.
DR   Pfam; PF01975; SurE; 1.
DR   SUPFAM; SSF64167; SSF64167; 1.
DR   TIGRFAMs; TIGR00087; surE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..254
FT                   /note="5'/3'-nucleotidase SurE"
FT                   /id="PRO_0000235673"
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         10
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         40
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT   BINDING         93
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
SQ   SEQUENCE   254 AA;  27289 MW;  C1BBACEC6F9B2661 CRC64;
     MIRILLSNDD GISAPGIQTL ASALREFAQV QIVAPDRNRS GASNALTLDS ALRITTLSNG
     DIAVQQGTPT DCVYLGVNAL MRPRPDIVVS GINAGPNLGD DVIYSGTVAA AMEGRHLGYP
     ALAVSLNGHQ HYDTAAAVTC RLLRALQRKP LRTGKILNIN VPDLPLSEIK GIRVTRCGSR
     HPAEQVFCQQ DPRGQDLYWI GPPGEKYDAG PDTDFAAVEQ GYVSITPLQV DLTAYTAQEV
     VESWLANTEV DGEW
 
 
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