MAZG_MYCS2
ID MAZG_MYCS2 Reviewed; 324 AA.
AC A0R3C4; I7GE40;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase;
DE Short=NTP-PPase;
DE EC=3.6.1.8;
GN Name=mazG; OrderedLocusNames=MSMEG_5422, MSMEI_5273;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION IN RESPONSE TO OXIDATIVE STRESS, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF ALA-222, DISRUPTION PHENOTYPE, INDUCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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).
CC -!- FUNCTION: Required to maintain the full capacity of the mycobacteria to
CC respond to oxidative stress via the degradation of the oxidation-
CC induced damaged nucleotides. It hydrolyzes all canonical (d)NTPs, as
CC well as the mutagenic dUTP and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-
CC triphosphate (8-oxo-dGTP). Also involved in the transcriptional
CC activation of RelA in response to oxidative stress.
CC {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=0.16 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=0.9 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 Vmax=0.16 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=3.1 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 -!- SUBUNIT: Homotetramer.
CC -!- INDUCTION: By oxidative stress. {ECO:0000269|PubMed:20529853}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show are defective in
CC response to oxidative stress. Complementation with mazG restores
CC resistance to oxidative stress. {ECO:0000269|PubMed:20529853}.
CC -!- SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase
CC family. {ECO:0000305}.
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DR EMBL; CP000480; ABK75736.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41716.1; -; Genomic_DNA.
DR RefSeq; WP_011730524.1; NZ_SIJM01000006.1.
DR RefSeq; YP_889662.1; NC_008596.1.
DR AlphaFoldDB; A0R3C4; -.
DR SMR; A0R3C4; -.
DR STRING; 246196.MSMEI_5273; -.
DR EnsemblBacteria; ABK75736; ABK75736; MSMEG_5422.
DR EnsemblBacteria; AFP41716; AFP41716; MSMEI_5273.
DR GeneID; 66736725; -.
DR KEGG; msg:MSMEI_5273; -.
DR KEGG; msm:MSMEG_5422; -.
DR PATRIC; fig|246196.19.peg.5284; -.
DR eggNOG; COG3956; Bacteria.
DR OMA; WESQQTH; -.
DR OrthoDB; 1099129at2; -.
DR SABIO-RK; A0R3C4; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047693; F:ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR004518; MazG_cat.
DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG.
DR PANTHER; PTHR30522; PTHR30522; 1.
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..324
FT /note="Nucleoside triphosphate pyrophosphohydrolase"
FT /id="PRO_0000401207"
FT MUTAGEN 222
FT /note="A->E: Pyrophosphohydrolase activity is reduced 30-
FT fold."
FT /evidence="ECO:0000269|PubMed:20529853"
SQ SEQUENCE 324 AA; 35303 MW; B65037152ED4F267 CRC64;
MIVVLVDPRR PALVPVDAVE FLTGDVQYTE EMPVKVPWSL PSARPAYDGE DAPVLLSSDP
EHPVVKARLA AGDRLIAAPE PQPGERLVDA VALMDKLRTS GPWESEQTHD SLRRYLLEET
YELFDAVRSG NADELREELG DVLLQVLFHA RIAEDAPHHP FSIDDVADAL VRKLGNRVPA
VLAGESISLD EQLAQWEERK AQEKKVKARA SSMDDVPTGQ PALALAQKVL ARVSQAGLPA
ELIPASLTSV SVSADTDSEN ELRTAVLEFM DTVREVEAAV AAGRRGEDVP EELDVAPLGV
ISEDEWRAYW PGAESSASEA EPEE
