MAZG_THEMA
ID MAZG_THEMA Reviewed; 255 AA.
AC Q9X015;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG;
DE Short=NTP-PPase;
DE EC=3.6.1.1 {ECO:0000269|PubMed:12657645};
DE EC=3.6.1.9 {ECO:0000269|PubMed:12657645};
GN Name=mazG; OrderedLocusNames=TM_0913;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION AS A PYROPHOSPHOHYDROLASE AND PYROPHOSPHATASE, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF GLU-41; GLU-42; GLU-45; GLU-61; ARG-97; ARG-98; LYS-118;
RP GLU-173; GLU-176 AND 185-GLU-GLU-186, MASS SPECTROMETRY, ACTIVITY
RP REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=12657645; DOI=10.1074/jbc.m213294200;
RA Zhang J., Zhang Y., Inouye M.;
RT "Thermotoga maritima MazG protein has both nucleoside triphosphate
RT pyrophosphohydrolase and pyrophosphatase activities.";
RL J. Biol. Chem. 278:21408-21414(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of all eight canonical
CC ribonucleoside triphosphates (NTP) and deoxyribonucleoside
CC triphosphates (dNTP) to their corresponding nucleoside monophosphates
CC ((d)NMP) and PPi and subsequently hydrolyzes the resultant PPi to Pi.
CC The NTPase activity with deoxyribonucleoside triphosphates as substrate
CC is higher than corresponding ribonucleoside triphosphates. dGTP is the
CC best substrate among the deoxyribonucleoside triphosphates, and GTP is
CC the best among the ribonucleoside triphosphates.
CC {ECO:0000269|PubMed:12657645}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC Evidence={ECO:0000269|PubMed:12657645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000269|PubMed:12657645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000269|PubMed:12657645};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by AMPCPP (alpha,beta-methyleneadenosine
CC triphosphate). {ECO:0000269|PubMed:12657645}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for CTP (at pH 8 and at 70 degrees Celsius);
CC KM=1 mM for dGTP (at pH 8 and at 70 degrees Celsius);
CC KM=1 mM for GTP (at pH 8 and at 70 degrees Celsius);
CC KM=1 mM for ATP (at pH 8 and at 70 degrees Celsius);
CC KM=1.1 mM for UTP (at pH 8 and at 70 degrees Celsius);
CC KM=1.5 mM for dTTP (at pH 8 and at 70 degrees Celsius);
CC KM=1.7 mM for dCTP (at pH 8 and at 70 degrees Celsius);
CC KM=3.2 mM for dATP (at pH 8 and at 70 degrees Celsius);
CC Vmax=0.22 nmol/min/ug enzyme with CTP as substrate (at pH 8 and at 70
CC degrees Celsius);
CC Vmax=0.36 nmol/min/ug enzyme with UTP as substrate (at pH 8 and at 70
CC degrees Celsius);
CC Vmax=0.39 nmol/min/ug enzyme with ATP as substrate (at pH 8 and at 70
CC degrees Celsius);
CC Vmax=1.30 nmol/min/ug enzyme with dTTP as substrate (at pH 8 and at
CC 70 degrees Celsius);
CC Vmax=1.39 nmol/min/ug enzyme with GTP as substrate (at pH 8 and at 70
CC degrees Celsius);
CC Vmax=1.90 nmol/min/ug enzyme with dGTP as substrate (at pH 8 and at
CC 70 degrees Celsius);
CC Vmax=2 nmol/min/ug enzyme with dCTP as substrate (at pH 8 and at 70
CC degrees Celsius);
CC Vmax=2.25 nmol/min/ug enzyme with dATP as substrate (at pH 8 and at
CC 70 degrees Celsius);
CC Temperature dependence:
CC Optimum temperature is about 80 degrees Celsius. MazG is very stable
CC at high temperature, and no change is detected up to 85 degrees
CC Celsius.;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=29728; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12657645};
CC -!- SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD35994.1; -; Genomic_DNA.
DR PIR; H72319; H72319.
DR RefSeq; NP_228721.1; NC_000853.1.
DR RefSeq; WP_004080649.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X015; -.
DR SMR; Q9X015; -.
DR STRING; 243274.THEMA_00070; -.
DR DNASU; 898587; -.
DR EnsemblBacteria; AAD35994; AAD35994; TM_0913.
DR KEGG; tma:TM0913; -.
DR eggNOG; COG3956; Bacteria.
DR InParanoid; Q9X015; -.
DR OMA; HPHIYGD; -.
DR OrthoDB; 1099129at2; -.
DR BRENDA; 3.6.1.1; 6331.
DR BRENDA; 3.6.1.9; 6331.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
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 ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..255
FT /note="Nucleoside triphosphate
FT pyrophosphohydrolase/pyrophosphatase MazG"
FT /id="PRO_0000413417"
FT BINDING 162..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 182..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 215..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 41
FT /note="E->Q: Reduces the NTPase activity to 10% of the
FT wild-type activity; when associated with Q-42."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 42
FT /note="E->Q: Reduces the NTPase activity to 10% of the
FT wild-type activity; when associated with Q-41."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 45
FT /note="E->Q: Reduces the NTPase activity to 10% of the
FT wild-type activity."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 61
FT /note="E->Q: Reduces the NTPase activity to 10% of the
FT wild-type activity."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 97
FT /note="R->A: Reduces the NTPase activity to 10% of the
FT wild-type activity; when associated with A-98."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 98
FT /note="R->A: Reduces the NTPase activity to 10% of the
FT wild-type activity; when associated with A-97."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 118
FT /note="K->E: Reduces the NTPase activity to 10% of the
FT wild-type activity."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 173
FT /note="E->A: Has little effects on the NTPase activity."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 176
FT /note="E->A: Has little effects on the NTPase activity."
FT /evidence="ECO:0000269|PubMed:12657645"
FT MUTAGEN 185..186
FT /note="EE->AA: Has little effects on the NTPase activity."
FT /evidence="ECO:0000269|PubMed:12657645"
SQ 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
