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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)DescriptionActionsGraphical viewLength
Metal bindingi172Magnesium1
Metal bindingi175Magnesium1
Binding sitei175ATP 11 Publication1
Metal bindingi193Magnesium1
Metal bindingi196Magnesium1
Binding sitei196ATP 11 Publication1
Binding sitei253ATP 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi168 – 172ATP 11 Publication5
Nucleotide bindingi189 – 192ATP 11 Publication4
Nucleotide bindingi222 – 226ATP 21 Publication5

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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10572. mazG.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95R → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi119K → A: Does not affect the nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi168K → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi171E → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi172E → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1
Mutagenesisi175E → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi189K → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi192E → A: Does not affect nucleotide pyrophosphohydrolysis activity. 1 Publication1
Mutagenesisi193E → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1
Mutagenesisi196D → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1
Mutagenesisi222K → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1
Mutagenesisi226R → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1
Mutagenesisi253W → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1
Mutagenesisi257K → A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000962481 – 263Nucleoside triphosphate pyrophosphohydrolaseAdd BLAST263

Proteomic databases

PaxDbiP0AEY3.
PRIDEiP0AEY3.

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 interactors.
DIPiDIP-48054N.
IntActiP0AEY3. 7 interactors.
MINTiMINT-1311211.
STRINGi511145.b2781.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 15Combined sources13
Turni17 – 19Combined sources3
Helixi24 – 26Combined sources3
Helixi29 – 48Combined sources20
Helixi52 – 74Combined sources23
Turni75 – 77Combined sources3
Helixi81 – 93Combined sources13
Helixi115 – 123Combined sources9
Beta strandi132 – 134Combined sources3
Beta strandi137 – 139Combined sources3
Helixi141 – 153Combined sources13
Turni154 – 156Combined sources3
Helixi162 – 181Combined sources20
Beta strandi182 – 184Combined sources3
Helixi187 – 207Combined sources21
Helixi212 – 236Combined sources25
Helixi249 – 258Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CRAX-ray2.10A/B1-263[»]
3CRCX-ray3.00A/B1-263[»]
ProteinModelPortaliP0AEY3.
SMRiP0AEY3.
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)DescriptionActionsGraphical viewLength
Sequence conflicti226Missing in AAA03240 (Ref. 1) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CRAX-ray2.10A/B1-263[»]
3CRCX-ray3.00A/B1-263[»]
ProteinModelPortaliP0AEY3.
SMRiP0AEY3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0AEY3.
PRIDEiP0AEY3.

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.

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: November 2, 2016
This is version 87 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.