NTPPB_NITMU
ID NTPPB_NITMU Reviewed; 198 AA.
AC Q2YA50;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Nmul_A1068;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB74371.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2YA50; -.
DR SMR; Q2YA50; -.
DR STRING; 323848.Nmul_A1068; -.
DR EnsemblBacteria; ABB74371; ABB74371; Nmul_A1068.
DR KEGG; nmu:Nmul_A1068; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_1_0_4; -.
DR OMA; CAGSFKA; -.
DR Proteomes; UP000002718; 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..198
FT /note="7-methyl-GTP pyrophosphatase"
FT /id="PRO_0000267358"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 18
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 76
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 160
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 198 AA; 21678 MW; BB1B67EF46C3FC8E CRC64;
MKTQQIAQQL ILGSSSIYRR DLLQRLQIPF DVSNPDIDET PLPGETPDAT AVRLAAAKTR
AVAATHPGAL IIGADQVAVF EGIQLGKPLN HLNATRQLQL IRGKEVSFYT ALCLFNSAQD
TTRARLVPSR VKFRLLSDRQ IENYLDKEQP YHCAASSKLE GLGIALIEHM EGEDPTALIG
LPLIALVEML TLEGVEIV