MAZG_ECOLI
ID MAZG_ECOLI Reviewed; 263 AA.
AC P0AEY3; P33646; Q2MA51;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase;
DE Short=NTP-PPase;
DE EC=3.6.1.8;
GN Name=mazG; OrderedLocusNames=b2781, JW2752;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Aizenman E., Glaser G.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, AND INTERACTION WITH
RP ERA.
RX PubMed=12218018; DOI=10.1128/jb.184.19.5323-5329.2002;
RA Zhang J., Inouye M.;
RT "MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era,
RT an essential GTPase in Escherichia coli.";
RL J. Bacteriol. 184:5323-5329(2002).
RN [5]
RP FUNCTION IN NUTRITIONAL STRESS RESPONSE, ACTIVITY REGULATION, AND OPERON
RP STRUCTURE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and
RC K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16390452; DOI=10.1111/j.1365-2958.2005.04956.x;
RA Gross M., Marianovsky I., Glaser G.;
RT "MazG -- a regulator of programmed cell death in Escherichia coli.";
RL Mol. Microbiol. 59:590-601(2006).
RN [6]
RP FUNCTION AS PYROPHOSPHOHYDROLASE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20529853; DOI=10.1074/jbc.m109.088872;
RA Lu L.D., Sun Q., Fan X.Y., Zhong Y., Yao Y.F., Zhao G.P.;
RT "Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in
RT oxidative stress response.";
RL J. Biol. Chem. 285:28076-28085(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-119/ALA-257 IN COMPLEX
RP WITH ATP, FUNCTION IN NUTRITIONAL STRESS RESPONSE, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ARG-95; LYS-119; LYS-168; GLU-171; GLU-172; GLU-175;
RP LYS-189; GLU-192; GLU-193; ASP-196; LYS-222; ARG-226; TRP-253 AND LYS-257,
RP AND SUBUNIT.
RX PubMed=18353782; DOI=10.1074/jbc.m800479200;
RA Lee S., Kim M.H., Kang B.S., Kim J.S., Kim G.H., Kim Y.G., Kim K.J.;
RT "Crystal structure of Escherichia coli MazG, the regulator of nutritional
RT stress response.";
RL J. Biol. Chem. 283:15232-15240(2008).
CC -!- FUNCTION: Involved in the regulation of bacterial cell survival under
CC conditions of nutritional stress. Regulates the type II MazE-MazF
CC toxin-antitoxin (TA) system which mediates programmed cell death (PCD).
CC This is achieved by lowering the cellular concentration of (p)ppGpp
CC produced by RelA under amino acid starvation, thus protecting the cell
CC from the toxicity of MazF. Reduction of (p)ppGpp can be achieved by
CC direct degradation of (p)ppGpp or by degradation of NTPs, which are
CC substrates for (p)ppGpp synthesis by RelA.
CC {ECO:0000269|PubMed:16390452, ECO:0000269|PubMed:18353782,
CC ECO:0000269|PubMed:20529853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.8;
CC Evidence={ECO:0000269|PubMed:12218018, ECO:0000269|PubMed:18353782};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by the MazE-MazF complex.
CC {ECO:0000269|PubMed:16390452}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for dATP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=0.71 mM for UTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=0.36 mM for 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC Vmax=0.23 nmol/min/ug enzyme for 8-oxo-dGTP (at pH 9.6 and at 37
CC degrees Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.9 nmol/min/ug enzyme for dATP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.9 nmol/min/ug enzyme for dUTP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC -!- SUBUNIT: Homodimer. Interacts with Era. {ECO:0000269|PubMed:12218018,
CC ECO:0000269|PubMed:18353782}.
CC -!- INTERACTION:
CC P0AEY3; P0AEH5: elaB; NbExp=2; IntAct=EBI-554166, EBI-552130;
CC P0AEY3; P0A6F5: groEL; NbExp=2; IntAct=EBI-554166, EBI-543750;
CC -!- INDUCTION: Part of the relA-mazE-mazF-mazG operon, there is also a
CC second mazE-mazF specific promoter which is negatively autoregulated.
CC -!- SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase
CC family. {ECO:0000305}.
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DR EMBL; J04039; AAA03240.1; -; Unassigned_DNA.
DR EMBL; U29580; AAA69291.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75823.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76855.1; -; Genomic_DNA.
DR PIR; A65060; A65060.
DR RefSeq; NP_417261.1; NC_000913.3.
DR RefSeq; WP_001071648.1; NZ_STEB01000030.1.
DR PDB; 3CRA; X-ray; 2.10 A; A/B=1-263.
DR PDB; 3CRC; X-ray; 3.00 A; A/B=1-263.
DR PDBsum; 3CRA; -.
DR PDBsum; 3CRC; -.
DR AlphaFoldDB; P0AEY3; -.
DR SMR; P0AEY3; -.
DR BioGRID; 4262299; 19.
DR BioGRID; 851584; 1.
DR DIP; DIP-48054N; -.
DR IntAct; P0AEY3; 7.
DR STRING; 511145.b2781; -.
DR jPOST; P0AEY3; -.
DR PaxDb; P0AEY3; -.
DR PRIDE; P0AEY3; -.
DR EnsemblBacteria; AAC75823; AAC75823; b2781.
DR EnsemblBacteria; BAE76855; BAE76855; BAE76855.
DR GeneID; 66673352; -.
DR GeneID; 947254; -.
DR KEGG; ecj:JW2752; -.
DR KEGG; eco:b2781; -.
DR PATRIC; fig|1411691.4.peg.3954; -.
DR EchoBASE; EB0567; -.
DR eggNOG; COG3956; Bacteria.
DR HOGENOM; CLU_038356_0_1_6; -.
DR InParanoid; P0AEY3; -.
DR OMA; HPHIYGD; -.
DR PhylomeDB; P0AEY3; -.
DR BioCyc; EcoCyc:EG10572-MON; -.
DR BioCyc; MetaCyc:EG10572-MON; -.
DR SABIO-RK; P0AEY3; -.
DR EvolutionaryTrace; P0AEY3; -.
DR PRO; PR:P0AEY3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047693; F:ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0009267; P:cellular response to starvation; IMP:EcoCyc.
DR GO; GO:0046061; P:dATP catabolic process; IBA:GO_Central.
DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
DR GO; GO:0046076; P:dTTP catabolic process; IBA:GO_Central.
DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
DR GO; GO:0046047; P:TTP catabolic process; IBA:GO_Central.
DR GO; GO:0046052; P:UTP catabolic process; IBA:GO_Central.
DR InterPro; IPR004518; MazG_cat.
DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG.
DR PANTHER; PTHR30522; PTHR30522; 1.
DR Pfam; PF03819; MazG; 2.
DR TIGRFAMs; TIGR00444; mazG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..263
FT /note="Nucleoside triphosphate pyrophosphohydrolase"
FT /id="PRO_0000096248"
FT BINDING 168..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18353782"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18353782"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 189..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18353782"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18353782"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 222..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18353782"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 95
FT /note="R->A: Does not affect nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 119
FT /note="K->A: Does not affect the nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 168
FT /note="K->A: Does not affect nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 171
FT /note="E->A: Does not affect nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 172
FT /note="E->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 175
FT /note="E->A: Does not affect nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 189
FT /note="K->A: Does not affect nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 192
FT /note="E->A: Does not affect nucleotide
FT pyrophosphohydrolysis activity."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 193
FT /note="E->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 196
FT /note="D->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 222
FT /note="K->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 226
FT /note="R->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 253
FT /note="W->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT MUTAGEN 257
FT /note="K->A: Loss of pyrophosphohydrolysis activity against
FT both ATP and dTTP."
FT /evidence="ECO:0000269|PubMed:18353782"
FT CONFLICT 226
FT /note="Missing (in Ref. 1; AAA03240)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:3CRA"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 29..48
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 52..74
FT /evidence="ECO:0007829|PDB:3CRA"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:3CRA"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3CRC"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3CRC"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:3CRA"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:3CRA"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 187..207
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 212..236
FT /evidence="ECO:0007829|PDB:3CRA"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:3CRA"
SQ SEQUENCE 263 AA; 30412 MW; C396BC3B9378D2BE CRC64;
MNQIDRLLTI MQRLRDPENG CPWDKEQTFA TIAPYTLEET YEVLDAIARE DFDDLRGELG
DLLFQVVFYA QMAQEEGRFD FNDICAAISD KLERRHPHVF ADSSAENSSE VLARWEQIKT
EERAQKAQHS ALDDIPRSLP ALMRAQKIQK RCANVGFDWT TLGPVVDKVY EEIDEVMYEA
RQAVVDQAKL EEEMGDLLFA TVNLARHLGT KAEIALQKAN EKFERRFREV ERIVAARGLE
MTGVDLETME EVWQQVKRQE IDL
