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Protein

Nucleoside triphosphate pyrophosphohydrolase

Gene

mazG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the regulation of bacterial cell survival under conditions of nutritional stress. Regulates the MazE-MazF toxin-antitoxin (TA) module that mediates programmed cell death (PCD). This is achieved by lowering the cellular concentration of (p)ppGpp produced by RelA under amino acid starvation, thus protecting the cell from the toxicity of MazF. Reduction of (p)ppGpp can be achieved by direct degradation of (p)ppGpp or by degradation of NTPs, which are substrates for (p)ppGpp synthesis by RelA.3 Publications

Catalytic activityi

ATP + H2O = AMP + diphosphate.2 Publications

Cofactori

Enzyme regulationi

Inhibited by the MazE-MazF complex.1 Publication

Kineticsi

  1. KM=0.34 mM for dATP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)1 Publication
  2. KM=0.71 mM for UTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)1 Publication
  3. KM=0.36 mM for 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)1 Publication
  1. Vmax=0.23 nmol/min/µg enzyme for 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)1 Publication
  2. Vmax=1.9 nmol/min/µg enzyme for dATP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)1 Publication
  3. Vmax=1.9 nmol/min/µg enzyme for dUTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Magnesium
Metal bindingi175 – 1751Magnesium
Binding sitei175 – 1751ATP 11 Publication
Metal bindingi193 – 1931Magnesium
Metal bindingi196 – 1961Magnesium
Binding sitei196 – 1961ATP 11 Publication
Binding sitei253 – 2531ATP 21 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 1725ATP 11 Publication
Nucleotide bindingi189 – 1924ATP 11 Publication
Nucleotide bindingi222 – 2265ATP 21 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10572-MONOMER.
ECOL316407:JW2752-MONOMER.
MetaCyc:EG10572-MONOMER.
RETL1328306-WGS:GSTH-2015-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside triphosphate pyrophosphohydrolase (EC:3.6.1.8)
Short name:
NTP-PPase
Gene namesi
Name:mazG
Ordered Locus Names:b2781, JW2752
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10572. mazG.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951R → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi119 – 1191K → A: Does not affect the nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi168 – 1681K → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi171 – 1711E → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi172 – 1721E → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication
Mutagenesisi175 – 1751E → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi189 – 1891K → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi192 – 1921E → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication
Mutagenesisi193 – 1931E → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication
Mutagenesisi196 – 1961D → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication
Mutagenesisi222 – 2221K → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication
Mutagenesisi226 – 2261R → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication
Mutagenesisi253 – 2531W → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication
Mutagenesisi257 – 2571K → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Nucleoside triphosphate pyrophosphohydrolasePRO_0000096248Add
BLAST

Proteomic databases

PaxDbiP0AEY3.

Expressioni

Inductioni

Part of the relA-mazE-mazF-mazG operon, there is also a second mazE-mazF specific promoter which is negatively autoregulated.

Interactioni

Subunit structurei

Homodimer. Interacts with Era.2 Publications

Protein-protein interaction databases

BioGridi4262299. 19 interactions.
DIPiDIP-48054N.
IntActiP0AEY3. 7 interactions.
MINTiMINT-1311211.
STRINGi511145.b2781.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513Combined sources
Turni17 – 193Combined sources
Helixi24 – 263Combined sources
Helixi29 – 4820Combined sources
Helixi52 – 7423Combined sources
Turni75 – 773Combined sources
Helixi81 – 9313Combined sources
Helixi115 – 1239Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Helixi141 – 15313Combined sources
Turni154 – 1563Combined sources
Helixi162 – 18120Combined sources
Beta strandi182 – 1843Combined sources
Helixi187 – 20721Combined sources
Helixi212 – 23625Combined sources
Helixi249 – 25810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CRAX-ray2.10A/B1-263[»]
3CRCX-ray3.00A/B1-263[»]
ProteinModelPortaliP0AEY3.
SMRiP0AEY3. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEY3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DXN. Bacteria.
COG1694. LUCA.
HOGENOMiHOG000272340.
InParanoidiP0AEY3.
KOiK04765.
OMAiRVGFDWE.
PhylomeDBiP0AEY3.

Family and domain databases

InterProiIPR004518. MazG_cat.
IPR011551. NTP_PyrPHydrolase_MazG.
[Graphical view]
PANTHERiPTHR30522:SF0. PTHR30522:SF0. 1 hit.
PfamiPF03819. MazG. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00444. mazG. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AEY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQIDRLLTI MQRLRDPENG CPWDKEQTFA TIAPYTLEET YEVLDAIARE
60 70 80 90 100
DFDDLRGELG DLLFQVVFYA QMAQEEGRFD FNDICAAISD KLERRHPHVF
110 120 130 140 150
ADSSAENSSE VLARWEQIKT EERAQKAQHS ALDDIPRSLP ALMRAQKIQK
160 170 180 190 200
RCANVGFDWT TLGPVVDKVY EEIDEVMYEA RQAVVDQAKL EEEMGDLLFA
210 220 230 240 250
TVNLARHLGT KAEIALQKAN EKFERRFREV ERIVAARGLE MTGVDLETME
260
EVWQQVKRQE IDL
Length:263
Mass (Da):30,412
Last modified:December 20, 2005 - v1
Checksum:iC396BC3B9378D2BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261Missing in AAA03240 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04039 Unassigned DNA. Translation: AAA03240.1.
U29580 Genomic DNA. Translation: AAA69291.1.
U00096 Genomic DNA. Translation: AAC75823.1.
AP009048 Genomic DNA. Translation: BAE76855.1.
PIRiA65060.
RefSeqiNP_417261.1. NC_000913.3.
WP_001071648.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75823; AAC75823; b2781.
BAE76855; BAE76855; BAE76855.
GeneIDi947254.
KEGGiecj:JW2752.
eco:b2781.
PATRICi32120978. VBIEscCol129921_2881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04039 Unassigned DNA. Translation: AAA03240.1.
U29580 Genomic DNA. Translation: AAA69291.1.
U00096 Genomic DNA. Translation: AAC75823.1.
AP009048 Genomic DNA. Translation: BAE76855.1.
PIRiA65060.
RefSeqiNP_417261.1. NC_000913.3.
WP_001071648.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CRAX-ray2.10A/B1-263[»]
3CRCX-ray3.00A/B1-263[»]
ProteinModelPortaliP0AEY3.
SMRiP0AEY3. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262299. 19 interactions.
DIPiDIP-48054N.
IntActiP0AEY3. 7 interactions.
MINTiMINT-1311211.
STRINGi511145.b2781.

Proteomic databases

PaxDbiP0AEY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75823; AAC75823; b2781.
BAE76855; BAE76855; BAE76855.
GeneIDi947254.
KEGGiecj:JW2752.
eco:b2781.
PATRICi32120978. VBIEscCol129921_2881.

Organism-specific databases

EchoBASEiEB0567.
EcoGeneiEG10572. mazG.

Phylogenomic databases

eggNOGiENOG4105DXN. Bacteria.
COG1694. LUCA.
HOGENOMiHOG000272340.
InParanoidiP0AEY3.
KOiK04765.
OMAiRVGFDWE.
PhylomeDBiP0AEY3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10572-MONOMER.
ECOL316407:JW2752-MONOMER.
MetaCyc:EG10572-MONOMER.
RETL1328306-WGS:GSTH-2015-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEY3.
PROiP0AEY3.

Family and domain databases

InterProiIPR004518. MazG_cat.
IPR011551. NTP_PyrPHydrolase_MazG.
[Graphical view]
PANTHERiPTHR30522:SF0. PTHR30522:SF0. 1 hit.
PfamiPF03819. MazG. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00444. mazG. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAZG_ECOLI
AccessioniPrimary (citable) accession number: P0AEY3
Secondary accession number(s): P33646, Q2MA51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.