MAZG_MYCTU
ID MAZG_MYCTU Reviewed; 325 AA.
AC P96379; L0T5L3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase;
DE Short=NTP-PPase;
DE EC=3.6.1.8;
GN Name=mazG; OrderedLocusNames=Rv1021;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS PYROPHOSPHOHYDROLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF ALA-219, INDUCTION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Required to maintain the full capacity of the mycobacterium
CC to respond to oxidative stress via the degradation of oxidation-induced
CC damaged nucleotides. Hydrolyzes all canonical (d)NTPs, as well as
CC mutagenic dUTP and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
CC (8-oxo-dGTP). Also involved in the transcriptional activation of RelA
CC in response to oxidative stress. {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:20529853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 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 KM=0.4 mM for GTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=0.4 mM for dGTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=0.6 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=0.6 mM for GTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 20 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=1.1 mM for dUTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=1.2 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=1.3 mM for dTTP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC KM=1.6 mM for ATP (at pH 9.6 and at 37 degrees Celsius in the
CC presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853};
CC Vmax=0.14 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=0.5 nmol/min/ug enzyme for UTP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.2 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 Vmax=1.3 nmol/min/ug enzyme for ATP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.4 nmol/min/ug enzyme for dGTP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.5 nmol/min/ug enzyme for GTP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.6 nmol/min/ug enzyme for dTTP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 5 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC Vmax=1.7 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=2.3 nmol/min/ug enzyme for GTP (at pH 9.6 and at 37 degrees
CC Celsius in the presence of 20 mM magnesium)
CC {ECO:0000269|PubMed:20529853};
CC pH dependence:
CC Optimum pH is 9.6. {ECO:0000269|PubMed:20529853};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. The activity is abolished
CC at 70 degrees Celsius. {ECO:0000269|PubMed:20529853};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20529853}.
CC -!- INDUCTION: By oxidative stress. {ECO:0000269|PubMed:20529853}.
CC -!- SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43771.1; -; Genomic_DNA.
DR PIR; H70622; H70622.
DR RefSeq; NP_215537.1; NC_000962.3.
DR RefSeq; WP_003405276.1; NZ_NVQJ01000018.1.
DR AlphaFoldDB; P96379; -.
DR SMR; P96379; -.
DR STRING; 83332.Rv1021; -.
DR PaxDb; P96379; -.
DR DNASU; 886052; -.
DR GeneID; 45424993; -.
DR GeneID; 886052; -.
DR KEGG; mtu:Rv1021; -.
DR TubercuList; Rv1021; -.
DR eggNOG; COG3956; Bacteria.
DR InParanoid; P96379; -.
DR OMA; WESQQTH; -.
DR PhylomeDB; P96379; -.
DR SABIO-RK; P96379; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047693; F:ATP diphosphatase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046061; P:dATP catabolic process; IDA:MTBBASE.
DR GO; GO:0006203; P:dGTP catabolic process; IDA:MTBBASE.
DR GO; GO:0046076; P:dTTP catabolic process; IDA:MTBBASE.
DR GO; GO:0046081; P:dUTP catabolic process; IDA:MTBBASE.
DR GO; GO:0051289; P:protein homotetramerization; IPI:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MTBBASE.
DR GO; GO:0046047; P:TTP catabolic process; IDA:MTBBASE.
DR GO; GO:0046052; P:UTP catabolic process; IDA:MTBBASE.
DR InterPro; IPR004518; MazG_cat.
DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG.
DR PANTHER; PTHR30522; PTHR30522; 2.
DR Pfam; PF03819; MazG; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..325
FT /note="Nucleoside triphosphate pyrophosphohydrolase"
FT /id="PRO_0000401206"
FT MOTIF 219
FT /note="Important for catalytic activity"
FT MUTAGEN 219
FT /note="A->E: Pyrophosphohydrolase activity is reduced 20-
FT fold. It affects the magnesium binding and the protein
FT structure."
FT /evidence="ECO:0000269|PubMed:20529853"
SQ SEQUENCE 325 AA; 35413 MW; 5F54377B761D1509 CRC64;
MIVVLVDPRR PTLVPVEAIE FLRGEVQYTE EMPVAVPWSL PAARSAHAGN DAPVLLSSDP
NHPAVITRLA AGARLISAPD SQRGERLVDA VAMMDKLRTA GPWESEQTHD SLRRYLLEET
YELLDAVRSG SVDQLREELG DLLLQVLFHA RIAEDASQSP FTIDDVADTL MRKLGNRAPG
VLAGESISLE DQLAQWEAAK ASEKARKSVA DDVHTGQPAL ALAQKVIQRA QKAGLPAHLI
PDEITSVSVS ADVDAENTLR TAVLDFIDRL RCAERAIAVA RRGSNVAEQL DVTPLGVITE
QEWLAHWPTA VNDSRGGSKK RKGMR
