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5'/3'-nucleotidase SurE (EC 3.1.3.5) (EC 3.1.3.6) (Exopolyphosphatase) (EC 3.6.1.11) (Nucleoside monophosphate phosphohydrolase) (Stationary-phase survival protein SurE)

 SURE_ECOLI              Reviewed;         253 AA.
P0A840; P36664; Q2MA85;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
28-MAR-2018, entry version 100.
RecName: Full=5'/3'-nucleotidase SurE;
EC=3.1.3.5;
EC=3.1.3.6;
AltName: Full=Exopolyphosphatase;
EC=3.6.1.11;
AltName: Full=Nucleoside monophosphate phosphohydrolase;
AltName: Full=Stationary-phase survival protein SurE;
Name=surE; Synonyms=ygbC; OrderedLocusNames=b2744, JW2714;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MP180;
PubMed=7928962; DOI=10.1128/jb.176.19.6015-6022.1994;
Li C., Ichikawa J.K., Ravetto J.J., Kuo H.-C., Fu J.C., Clarke S.;
"A new gene involved in stationary-phase survival located at 59
minutes on the Escherichia coli chromosome.";
J. Bacteriol. 176:6015-6022(1994).
[2]
SEQUENCE REVISION.
Ichikawa J.K.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
FUNCTION, CHARACTERIZATION, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=15489502; DOI=10.1074/jbc.M411023200;
Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H.,
Savchenko A., Yakunin A.F.;
"General enzymatic screens identify three new nucleotidases in
Escherichia coli. Biochemical characterization of SurE, YfbR, and
YjjG.";
J. Biol. Chem. 279:54687-54694(2004).
-!- FUNCTION: Nucleotidase with a broad substrate specificity as it
can dephosphorylate various ribo- and deoxyribonucleoside 5'-
monophosphates and ribonucleoside 3'-monophosphates with highest
affinity to 3'-AMP. Also hydrolyzes polyphosphate
(exopolyphosphatase activity) with the preference for short-chain-
length substrates (P20-25). Might be involved in the regulation of
dNTP and NTP pools, and in the turnover of 3'-mononucleotides
produced by numerous intracellular RNases (T1, T2, and F) during
the degradation of various RNAs. Also plays a significant
physiological role in stress-response and is required for the
survival of E.coli in stationary growth phase.
{ECO:0000269|PubMed:15489502}.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate.
-!- CATALYTIC ACTIVITY: A 3'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate.
-!- CATALYTIC ACTIVITY: (Polyphosphate)(n) + H(2)O =
(polyphosphate)(n-1) + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15489502};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:15489502};
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Evidence={ECO:0000269|PubMed:15489502};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15489502};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:15489502};
Note=Binds 1 divalent metal cation per subunit. Highest
nucleotidase activity with Mn(2+), followed by Co(2+), Ni(2+) and
Mg(2+). Highest exopolyphosphatase activity with Mg(2+), followed
by Co(2+) and Zn(2+). {ECO:0000269|PubMed:15489502};
-!- ENZYME REGULATION: Inhibited by various ribo- or
deoxyribonucleoside 5'-triphosphates but is insensitive to
nucleoside diphosphates.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.32 mM for 5'-AMP {ECO:0000269|PubMed:15489502};
KM=0.26 mM for 5'-GMP {ECO:0000269|PubMed:15489502};
KM=0.28 mM for 5'-dGMP {ECO:0000269|PubMed:15489502};
KM=0.10 mM for 3'-AMP {ECO:0000269|PubMed:15489502};
KM=0.37 mM for 3'-CMP {ECO:0000269|PubMed:15489502};
KM=2.49 mM for pNPP {ECO:0000269|PubMed:15489502};
KM=0.02 mM for polyphosphate {ECO:0000269|PubMed:15489502};
Vmax=10.0 umol/min/mg enzyme with 5'-AMP as substrate
{ECO:0000269|PubMed:15489502};
Vmax=22.4 umol/min/mg enzyme with 5'-GMP as substrate
{ECO:0000269|PubMed:15489502};
Vmax=16.4 umol/min/mg enzyme with 5'-dGMP as substrate
{ECO:0000269|PubMed:15489502};
Vmax=20.1 umol/min/mg enzyme with 3'-AMP as substrate
{ECO:0000269|PubMed:15489502};
Vmax=12.1 umol/min/mg enzyme with 3'-CMP as substrate
{ECO:0000269|PubMed:15489502};
Vmax=7.24 umol/min/mg enzyme with pNPP as substrate
{ECO:0000269|PubMed:15489502};
Vmax=0.10 umol/min/mg enzyme with polyphosphate as substrate
{ECO:0000269|PubMed:15489502};
pH dependence:
Optimum pH is 7.0-7.2 for nucleotidase activity.
{ECO:0000269|PubMed:15489502};
-!- SUBUNIT: Monomer and homooligomer in solution. The oligomeric
complex consists of at least four subunits.
{ECO:0000269|PubMed:15489502}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the SurE nucleotidase family.
{ECO:0000305}.
-!- CAUTION: Was originally annotated as an acid phosphatase (EC
3.1.3.2). {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA69254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L07942; AAA79839.1; -; Genomic_DNA.
EMBL; U29579; AAA69254.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC75786.1; -; Genomic_DNA.
EMBL; AP009048; BAE76821.1; -; Genomic_DNA.
PIR; I69732; I69732.
RefSeq; NP_417224.1; NC_000913.3.
RefSeq; WP_001295182.1; NZ_LN832404.1.
ProteinModelPortal; P0A840; -.
SMR; P0A840; -.
BioGrid; 4262277; 12.
DIP; DIP-47982N; -.
IntAct; P0A840; 3.
STRING; 316385.ECDH10B_2912; -.
EPD; P0A840; -.
PaxDb; P0A840; -.
PRIDE; P0A840; -.
EnsemblBacteria; AAC75786; AAC75786; b2744.
EnsemblBacteria; BAE76821; BAE76821; BAE76821.
GeneID; 947211; -.
KEGG; ecj:JW2714; -.
KEGG; eco:b2744; -.
PATRIC; fig|511145.12.peg.2839; -.
EchoBASE; EB1764; -.
EcoGene; EG11817; surE.
eggNOG; ENOG4105CV2; Bacteria.
eggNOG; COG0496; LUCA.
HOGENOM; HOG000122500; -.
InParanoid; P0A840; -.
KO; K03787; -.
OMA; DCVHIAL; -.
PhylomeDB; P0A840; -.
BioCyc; EcoCyc:EG11817-MONOMER; -.
BioCyc; MetaCyc:EG11817-MONOMER; -.
BRENDA; 3.1.3.5; 2026.
BRENDA; 3.1.3.6; 2026.
BRENDA; 3.6.1.11; 2026.
SABIO-RK; P0A840; -.
PRO; PR:P0A840; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008254; F:3'-nucleotidase activity; IDA:EcoCyc.
GO; GO:0008253; F:5'-nucleotidase activity; IDA:EcoCyc.
GO; GO:0004309; F:exopolyphosphatase activity; IDA:EcoCyc.
GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0046050; P:UMP catabolic process; IGI:EcoCyc.
Gene3D; 3.40.1210.10; -; 1.
HAMAP; MF_00060; SurE; 1.
InterPro; IPR030048; SurE.
InterPro; IPR002828; SurE-like_Pase/nucleotidase.
InterPro; IPR036523; SurE-like_sf.
Pfam; PF01975; SurE; 1.
TIGRFAMs; TIGR00087; surE; 1.
1: Evidence at protein level;
Cobalt; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese;
Metal-binding; Nickel; Nucleotide-binding; Reference proteome; Zinc.
CHAIN 1 253 5'/3'-nucleotidase SurE.
/FTId=PRO_0000111809.
METAL 8 8 Divalent metal cation. {ECO:0000250}.
METAL 9 9 Divalent metal cation. {ECO:0000250}.
METAL 39 39 Divalent metal cation. {ECO:0000250}.
METAL 92 92 Divalent metal cation. {ECO:0000250}.
SEQUENCE 253 AA; 26900 MW; 33A7CD0AEE13C3DB CRC64;
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD
IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA
LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH
PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV
SDWLNSVGVG TQW


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