NTPPB_PSEU2
ID NTPPB_PSEU2 Reviewed; 192 AA.
AC Q4ZVY2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
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=Psyr_1642;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY36690.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000075; AAY36690.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024661285.1; NC_007005.1.
DR RefSeq; YP_234728.1; NC_007005.1.
DR AlphaFoldDB; Q4ZVY2; -.
DR SMR; Q4ZVY2; -.
DR STRING; 205918.Psyr_1642; -.
DR EnsemblBacteria; AAY36690; AAY36690; Psyr_1642.
DR KEGG; psb:Psyr_1642; -.
DR PATRIC; fig|205918.7.peg.1679; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_1_0_6; -.
DR Proteomes; UP000000426; 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.
FT CHAIN 1..192
FT /note="7-methyl-GTP pyrophosphatase"
FT /id="PRO_0000269481"
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; 21119 MW; 95B4AEDECC1F64A9 CRC64;
MPSLLLASSS SYRRELLARL RLPFTCRSPD IDESRRPDEA AFDLVQRLAR EKAEALTAEH
HHHLIIGSDQ VAVLDEQVLG KPHSFERALE QLTAASGKSV TFLTGLALFN SSTGECQVDC
VPFTVHMREL DRASIERYLH AEQPYDCAGS FKAEGLGVSL FRSTEGSDAT SLIGLPLIRL
VDMLIKEGVS VP