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Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG (NTP-PPase) (EC 3.6.1.1) (EC 3.6.1.9)

 MAZG_THEMA              Reviewed;         255 AA.
Q9X015;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-JUN-2017, entry version 84.
RecName: Full=Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG;
Short=NTP-PPase;
EC=3.6.1.1 {ECO:0000269|PubMed:12657645};
EC=3.6.1.9 {ECO:0000269|PubMed:12657645};
Name=mazG; OrderedLocusNames=TM_0913;
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[2]
FUNCTION AS A PYROPHOSPHOHYDROLASE AND PYROPHOSPHATASE, CATALYTIC
ACTIVITY, MUTAGENESIS OF GLU-41; GLU-42; GLU-45; GLU-61; ARG-97;
ARG-98; LYS-118; GLU-173; GLU-176 AND 185-GLU-GLU-186, MASS
SPECTROMETRY, ENZYME REGULATION, AND SUBSTRATE SPECIFICITY.
PubMed=12657645; DOI=10.1074/jbc.M213294200;
Zhang J., Zhang Y., Inouye M.;
"Thermotoga maritima MazG protein has both nucleoside triphosphate
pyrophosphohydrolase and pyrophosphatase activities.";
J. Biol. Chem. 278:21408-21414(2003).
-!- FUNCTION: Catalyzes the hydrolysis of all eight canonical
ribonucleoside triphosphates (NTP) and deoxyribonucleoside
triphosphates (dNTP) to their corresponding nucleoside
monophosphates ((d)NMP) and PPi and subsequently hydrolyzes the
resultant PPi to Pi. The NTPase activity with deoxyribonucleoside
triphosphates as substrate is higher than corresponding
ribonucleoside triphosphates. dGTP is the best substrate among the
deoxyribonucleoside triphosphates, and GTP is the best among the
ribonucleoside triphosphates. {ECO:0000269|PubMed:12657645}.
-!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
{ECO:0000269|PubMed:12657645}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000269|PubMed:12657645}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by AMPCPP (alpha,beta-
methyleneadenosine triphosphate). {ECO:0000269|PubMed:12657645}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.4 mM for CTP (at pH 8 and at 70 degrees Celsius);
KM=1 mM for dGTP (at pH 8 and at 70 degrees Celsius);
KM=1 mM for GTP (at pH 8 and at 70 degrees Celsius);
KM=1 mM for ATP (at pH 8 and at 70 degrees Celsius);
KM=1.1 mM for UTP (at pH 8 and at 70 degrees Celsius);
KM=1.5 mM for dTTP (at pH 8 and at 70 degrees Celsius);
KM=1.7 mM for dCTP (at pH 8 and at 70 degrees Celsius);
KM=3.2 mM for dATP (at pH 8 and at 70 degrees Celsius);
Vmax=0.22 nmol/min/ug enzyme with CTP as substrate (at pH 8 and
at 70 degrees Celsius);
Vmax=0.36 nmol/min/ug enzyme with UTP as substrate (at pH 8 and
at 70 degrees Celsius);
Vmax=0.39 nmol/min/ug enzyme with ATP as substrate (at pH 8 and
at 70 degrees Celsius);
Vmax=1.30 nmol/min/ug enzyme with dTTP as substrate (at pH 8 and
at 70 degrees Celsius);
Vmax=1.39 nmol/min/ug enzyme with GTP as substrate (at pH 8 and
at 70 degrees Celsius);
Vmax=1.90 nmol/min/ug enzyme with dGTP as substrate (at pH 8 and
at 70 degrees Celsius);
Vmax=2 nmol/min/ug enzyme with dCTP as substrate (at pH 8 and at
70 degrees Celsius);
Vmax=2.25 nmol/min/ug enzyme with dATP as substrate (at pH 8 and
at 70 degrees Celsius);
Temperature dependence:
Optimum temperature is about 80 degrees Celsius. MazG is very
stable at high temperature, and no change is detected up to 85
degrees Celsius.;
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=29728; Method=Electrospray; Range=2-255;
Evidence={ECO:0000269|PubMed:12657645};
-!- SIMILARITY: Belongs to the nucleoside triphosphate
pyrophosphohydrolase family. {ECO:0000305}.
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EMBL; AE000512; AAD35994.1; -; Genomic_DNA.
PIR; H72319; H72319.
RefSeq; NP_228721.1; NC_000853.1.
RefSeq; WP_004080649.1; NZ_CP011107.1.
ProteinModelPortal; Q9X015; -.
SMR; Q9X015; -.
STRING; 243274.TM0913; -.
DNASU; 898587; -.
EnsemblBacteria; AAD35994; AAD35994; TM_0913.
GeneID; 898587; -.
KEGG; tma:TM0913; -.
eggNOG; ENOG4105DXN; Bacteria.
eggNOG; COG1694; LUCA.
InParanoid; Q9X015; -.
KO; K02499; -.
OMA; HPHIYGD; -.
Proteomes; UP000008183; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
GO; GO:0046061; P:dATP catabolic process; IBA:GO_Central.
GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
GO; GO:0046076; P:dTTP catabolic process; IBA:GO_Central.
GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
GO; GO:0046047; P:TTP catabolic process; IBA:GO_Central.
GO; GO:0046052; P:UTP catabolic process; IBA:GO_Central.
InterPro; IPR004518; MazG_cat.
InterPro; IPR011551; NTP_PyrPHydrolase_MazG.
Pfam; PF03819; MazG; 2.
TIGRFAMs; TIGR00444; mazG; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Nucleotide-binding; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 255 Nucleoside triphosphate
pyrophosphohydrolase/pyrophosphatase
MazG.
/FTId=PRO_0000413417.
NP_BIND 162 166 ATP 1. {ECO:0000250}.
NP_BIND 182 185 ATP 1. {ECO:0000250}.
NP_BIND 215 219 ATP 2. {ECO:0000250}.
METAL 169 169 Magnesium. {ECO:0000250}.
METAL 186 186 Magnesium. {ECO:0000250}.
METAL 189 189 Magnesium. {ECO:0000250}.
BINDING 169 169 ATP 1. {ECO:0000250}.
BINDING 189 189 ATP 1. {ECO:0000250}.
BINDING 246 246 ATP 2. {ECO:0000250}.
MUTAGEN 41 41 E->Q: Reduces the NTPase activity to 10%
of the wild-type activity; when
associated with Q-42.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 42 42 E->Q: Reduces the NTPase activity to 10%
of the wild-type activity; when
associated with Q-41.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 45 45 E->Q: Reduces the NTPase activity to 10%
of the wild-type activity.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 61 61 E->Q: Reduces the NTPase activity to 10%
of the wild-type activity.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 97 97 R->A: Reduces the NTPase activity to 10%
of the wild-type activity; when
associated with A-98.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 98 98 R->A: Reduces the NTPase activity to 10%
of the wild-type activity; when
associated with A-97.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 118 118 K->E: Reduces the NTPase activity to 10%
of the wild-type activity.
{ECO:0000269|PubMed:12657645}.
MUTAGEN 173 173 E->A: Has little effects on the NTPase
activity. {ECO:0000269|PubMed:12657645}.
MUTAGEN 176 176 E->A: Has little effects on the NTPase
activity. {ECO:0000269|PubMed:12657645}.
MUTAGEN 185 186 EE->AA: Has little effects on the NTPase
activity. {ECO:0000269|PubMed:12657645}.
SEQUENCE 255 AA; 29805 MW; 92F4981444C70F42 CRC64;
MKEAGILFEE LVSIMEKLRS PEGCEWDRKQ THESLKPYLI EECYELIEAI DEKNDDMMKE
ELGDVLLQVV FHAQIARERG AFTIEDVIRT LNEKLIRRHP HVFGDSPGYS YKQWEDIKAQ
EKGKKKSSRI GEINPLVPAL SMARRIQENA SQVGFDWKDP EGVYEKIEEE LKELKEAKDP
RELEEEFGDL LFSIVNLSRF LNVDPESALR KATRKFVERF KKMEELIEKD GLVLEELPIE
KLDEYWEKAK GGDET


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