NTPPB_PECAS
ID NTPPB_PECAS Reviewed; 197 AA.
AC Q6D694;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=ECA1791;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG74696.1; -; Genomic_DNA.
DR RefSeq; WP_011093367.1; NC_004547.2.
DR AlphaFoldDB; Q6D694; -.
DR SMR; Q6D694; -.
DR STRING; 218491.ECA1791; -.
DR EnsemblBacteria; CAG74696; CAG74696; ECA1791.
DR GeneID; 57209498; -.
DR KEGG; eca:ECA1791; -.
DR PATRIC; fig|218491.5.peg.1819; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_1_0_6; -.
DR OMA; CAGSFKA; -.
DR OrthoDB; 1469203at2; -.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:InterPro.
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..197
FT /note="7-methyl-GTP pyrophosphatase"
FT /id="PRO_0000267307"
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 197 AA; 21606 MW; 376B29A7709F1276 CRC64;
MQQIVLASTS PYRKALLEKL TVPFVCASPD IDETPRIGEN AIDLVIRLAE SKARALATHY
TNHLIIGSDQ VCVLGNSITG KPHNKINATR QLQQASGKCV SFFTGLALFN SATQSIQSIA
EPFDVYFRTL TEAEIDGYLE KEQPWNCAGS FKSEGLGITL FERLSGRDPN TLIGLPLIAL
TQMLQKEGLN PLTVRNE