NTPPB_SALTY
ID NTPPB_SALTY Reviewed; 194 AA.
AC P58627;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=7-methyl-GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE Short=m(7)GTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000269|PubMed:24210219};
GN Name=yceF; OrderedLocusNames=STM1189;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24210219; DOI=10.1016/j.chembiol.2013.09.011;
RA Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X.,
RA Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N.,
RA Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G.,
RA Yakunin A.F.;
RT "Biochemical and structural studies of conserved Maf proteins revealed
RT nucleotide pyrophosphatases with a preference for modified nucleotides.";
RL Chem. Biol. 20:1386-1398(2013).
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-
CC methyl-GTP (m(7)GTP) (PubMed:24210219). May have a dual role in cell
CC division arrest and in preventing the incorporation of modified
CC nucleotides into cellular nucleic acids (PubMed:24210219).
CC {ECO:0000269|PubMed:24210219}.
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 ECO:0000269|PubMed:24210219};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30.9 uM for m(7)GTP {ECO:0000269|PubMed:24210219};
CC Note=kcat is 1.5 sec(-1). {ECO:0000269|PubMed:24210219};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Maf family. YceF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305|PubMed:24210219}.
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DR EMBL; AE006468; AAL20118.1; -; Genomic_DNA.
DR RefSeq; NP_460159.1; NC_003197.2.
DR RefSeq; WP_001137605.1; NC_003197.2.
DR AlphaFoldDB; P58627; -.
DR SMR; P58627; -.
DR STRING; 99287.STM1189; -.
DR PaxDb; P58627; -.
DR EnsemblBacteria; AAL20118; AAL20118; STM1189.
DR GeneID; 1252707; -.
DR KEGG; stm:STM1189; -.
DR PATRIC; fig|99287.12.peg.1258; -.
DR HOGENOM; CLU_040416_1_0_6; -.
DR OMA; CAGSFKA; -.
DR PhylomeDB; P58627; -.
DR BioCyc; SENT99287:STM1189-MON; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT CHAIN 1..194
FT /note="7-methyl-GTP pyrophosphatase"
FT /id="PRO_0000122979"
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 ECO:0000305|PubMed:24210219"
FT SITE 70
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 154
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
SQ SEQUENCE 194 AA; 21493 MW; 6B4B6A5E6CFA1649 CRC64;
MPRLILASTS PWRRALLEKL TIPFECAAPD VDETPMPGEA PRQLVLRLAQ AKAQSLAARF
PNHLIIGSDQ ICVLDGEITG KPLTEEKARQ QLAKASGNIV TFYTGLALYN SASGHLQTEV
EPFDVHFRHL SEAEIDDYVR KEHPLHCAGS FKSEGLGIAL FERLEGRDPN TLIGLPLIAL
CQMLRREGFN PLQQ
