NTPPB_BORA1
ID NTPPB_BORA1 Reviewed; 197 AA.
AC Q2KUK9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=BAV1115;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ48724.1; -; Genomic_DNA.
DR RefSeq; WP_012416799.1; NC_010645.1.
DR AlphaFoldDB; Q2KUK9; -.
DR SMR; Q2KUK9; -.
DR STRING; 360910.BAV1115; -.
DR EnsemblBacteria; CAJ48724; CAJ48724; BAV1115.
DR GeneID; 41393019; -.
DR KEGG; bav:BAV1115; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_1_0_4; -.
DR OMA; CAGSFKA; -.
DR OrthoDB; 1469203at2; -.
DR Proteomes; UP000001977; 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_0000267257"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 15
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 73
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 155
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 197 AA; 21254 MW; C801F0A131102F17 CRC64;
MHQNPRLILA SSSRYRRAML ERLRLPFESI SPDVDETPQA GEAPAALALR LSVAKAMAVA
RLHPGCIVIG SDQVATVDGQ PIGKPGDFAR AKSQLRQLSG RIVEFHSALA VTDGQRTEQA
DVITYCEFRP LTDAAIDAYL RAEEPYDTAG SAKAEGLGIT LMESMRSDDP TAIIGLPLIA
LTGMLRRFGL DPLRSPS