ID   NTPPB_PSEAE             Reviewed;         192 AA.
AC   Q9HZN2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=7-methyl-GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            Short=m(7)GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00528};
GN   OrderedLocusNames=PA2972;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-
CC       methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and
CC       in preventing the incorporation of modified nucleotides into cellular
CC       nucleic acids. {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP;
CC         Xref=Rhea:RHEA:58744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58285, ChEBI:CHEBI:87133;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- SIMILARITY: Belongs to the Maf family. YceF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00528}.
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DR   EMBL; AE004091; AAG06360.1; -; Genomic_DNA.
DR   PIR; D83273; D83273.
DR   RefSeq; NP_251662.1; NC_002516.2.
DR   RefSeq; WP_003113992.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZN2; -.
DR   SMR; Q9HZN2; -.
DR   STRING; 287.DR97_4967; -.
DR   PaxDb; Q9HZN2; -.
DR   PRIDE; Q9HZN2; -.
DR   DNASU; 879799; -.
DR   EnsemblBacteria; AAG06360; AAG06360; PA2972.
DR   GeneID; 879799; -.
DR   KEGG; pae:PA2972; -.
DR   PATRIC; fig|208964.12.peg.3118; -.
DR   PseudoCAP; PA2972; -.
DR   HOGENOM; CLU_040416_1_0_6; -.
DR   InParanoid; Q9HZN2; -.
DR   OMA; CAGSFKA; -.
DR   PhylomeDB; Q9HZN2; -.
DR   BioCyc; PAER208964:G1FZ6-3024-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00555; Maf; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00528; Maf; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR003697; Maf-like.
DR   PANTHER; PTHR43213; PTHR43213; 1.
DR   Pfam; PF02545; Maf; 1.
DR   PIRSF; PIRSF006305; Maf; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00172; maf; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..192
FT                   /note="7-methyl-GTP pyrophosphatase"
FT                   /id="PRO_0000123044"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            12
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            70
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            154
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   192 AA;  21054 MW;  F42BFE17D23BF74E CRC64;
     MPDLILASSS PYRRELLTRL RLPFESASPD IDESHRAGES AEELVRRLSA SKAEALAGRY
     PQHLVIGSDQ VAVLDGNILG KPHTPERAIQ QLRDASGKSV TFLTGLALLN SASRRIQVAC
     VPFTVHFRHL DESRIRRYVE AERPLDCAGS FKAEGLGVSL FRSTEGEDAT SLVGLPLIRL
     VDMLLEEGVE IP