MAZG_HAEIN
ID MAZG_HAEIN Reviewed; 263 AA.
AC P44723;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase;
DE Short=NTP-PPase;
DE EC=3.6.1.8;
GN Name=mazG; OrderedLocusNames=HI_0460;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Involved in the regulation of bacterial cell survival under
CC conditions of nutritional stress. Regulates the MazE-MazF toxin-
CC antitoxin (TA) system that mediates programmed cell death (PCD). This
CC is achieved by lowering the cellular concentration of (p)ppGpp produced
CC by RelA under amino acid starvation, thus protecting the cell from the
CC toxicity of MazF. Reduction of (p)ppGpp can be achieved by direct
CC degradation of (p)ppGpp or by degradation of NTPs, which are substrates
CC for (p)ppGpp synthesis by RelA (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase
CC family. {ECO:0000305}.
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DR EMBL; L42023; AAC22118.1; -; Genomic_DNA.
DR PIR; H64069; H64069.
DR RefSeq; NP_438621.1; NC_000907.1.
DR RefSeq; WP_005693705.1; NC_000907.1.
DR AlphaFoldDB; P44723; -.
DR SMR; P44723; -.
DR STRING; 71421.HI_0460; -.
DR EnsemblBacteria; AAC22118; AAC22118; HI_0460.
DR KEGG; hin:HI_0460; -.
DR PATRIC; fig|71421.8.peg.480; -.
DR eggNOG; COG3956; Bacteria.
DR HOGENOM; CLU_038356_0_1_6; -.
DR OMA; HPHIYGD; -.
DR PhylomeDB; P44723; -.
DR BioCyc; HINF71421:G1GJ1-476-MON; -.
DR Proteomes; UP000000579; 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 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 3: Inferred from homology;
KW ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..263
FT /note="Nucleoside triphosphate pyrophosphohydrolase"
FT /id="PRO_0000096250"
FT BINDING 170..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 191..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 224..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 30520 MW; B397803562943121 CRC64;
MRYSIQDFIQ LIAQLRNPNG GCPWDLKQNY ESMISCLTEE TYEVIEAIEK KDIPNLREEL
GDLLLQVVFF SQLAREDKYF AFDDVLQDVA EKIVRRHPHV FGDAKAGDET EALSRWNEMK
AKEKQGKSEE TSILDNVPRA LPSLTRAAKL QKRCSKVGFD WEEISPVFDK VREELEEVQA
EINRTSIEQN KVEEEIGDLL FATVNLARHL KCDPEDALRK ANLKFERRFR AVEQAVQQQG
KQVNNVPLIE LDLLWDEVKK QEN
