ID A0A0G9F718_LACPN Unreviewed; 202 AA.
AC A0A0G9F718;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405};
GN Name=rdgB {ECO:0000313|EMBL:ODO62100.1};
GN ORFNames=ASV54_09270 {ECO:0000313|EMBL:APD01517.1}, AVR83_11355
GN {ECO:0000313|EMBL:AOB23516.1}, C7M36_02308
GN {ECO:0000313|EMBL:QHM38023.1}, C7M40_00141
GN {ECO:0000313|EMBL:QHM48243.1}, Lp19_1992
GN {ECO:0000313|EMBL:KZU94018.1}, LPJSA22_02105
GN {ECO:0000313|EMBL:ODO62100.1}, LpLQ80_10215
GN {ECO:0000313|EMBL:AWI40862.1}, SN35N_2717
GN {ECO:0000313|EMBL:BBA83096.1};
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590 {ECO:0000313|EMBL:ODO62100.1, ECO:0000313|Proteomes:UP000094892};
RN [1] {ECO:0000313|Proteomes:UP000183026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA McLeod A., Rud I., Axelsson L.;
RT "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT associated with unfavorable effect.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOB23516.1, ECO:0000313|Proteomes:UP000093296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF {ECO:0000313|EMBL:AOB23516.1,
RC ECO:0000313|Proteomes:UP000093296};
RA Petkau K., Fast D., Duggal A., Foley E.;
RT "Comparative evaluation of the genomes of common bacterial members of the
RT Drosophila intestinal community.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KZU94018.1, ECO:0000313|Proteomes:UP000076882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19.1 {ECO:0000313|EMBL:KZU94018.1,
RC ECO:0000313|Proteomes:UP000076882};
RA Martino M.E.;
RT "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT uncoupling from niche constraints.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ODO62100.1, ECO:0000313|Proteomes:UP000094892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSA22 {ECO:0000313|EMBL:ODO62100.1,
RC ECO:0000313|Proteomes:UP000094892};
RA Choi H.S.;
RT "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT fermented soybean paste.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BBA83096.1, ECO:0000313|Proteomes:UP000269784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN35N {ECO:0000313|EMBL:BBA83096.1,
RC ECO:0000313|Proteomes:UP000269784};
RX PubMed=29607926; DOI=.1248/bpb.b17-00840;
RA Noda M., Shiraga M., Kumagai T., Danshiitsoodol N., Sugiyama M.;
RT "Characterization of the SN35N Strain-Specific Exopolysaccharide Encoded in
RT the Whole Circular Genome of a Plant-Derived Lactobacillus plantarum.";
RL Biol. Pharm. Bull. 41:536-545(2018).
RN [6] {ECO:0000313|EMBL:QHM38023.1, ECO:0000313|Proteomes:UP000464882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101167 {ECO:0000313|EMBL:QHM38023.1,
RC ECO:0000313|Proteomes:UP000464882};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101167 having anti-virus activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QHM48243.1, ECO:0000313|Proteomes:UP000465032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM48243.1,
RC ECO:0000313|Proteomes:UP000465032};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AWI40862.1, ECO:0000313|Proteomes:UP000244922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ80 {ECO:0000313|EMBL:AWI40862.1,
RC ECO:0000313|Proteomes:UP000244922};
RA Moriya N., Nakano K., Shiroma A., Shinzato M., Ashimine N., Minami M.,
RA Tamotsu H., Shimoji M., Nakanishi T., Ohki S., Teruya K., Satou K.,
RA Hirano T., Hagi T., Kobayashi M., Nomura M., Kimoto H.N., Tajima K.,
RA Cai Y., Suzuki C.;
RT "Complete Genome Sequence of Lactobacillus plantarum Strain LQ80 Selected
RT for Preparation of Fermented Liquid Feed for Pig.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|EMBL:APD01517.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MF1298 {ECO:0000313|EMBL:APD01517.1};
RA McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT associated with unfavorable effect.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside
CC triphosphates to their monophosphate derivatives, with a high
CC preference for the non-canonical purine nucleotides XTP (xanthosine
CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to
CC function as a house-cleaning enzyme that removes non-canonical purine
CC nucleotides from the nucleotide pool, thus preventing their
CC incorporation into DNA/RNA and avoiding chromosomal lesions.
CC {ECO:0000256|HAMAP-Rule:MF_01405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405,
CC ECO:0000256|RuleBase:RU003781}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}.
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DR EMBL; CP013753; AOB23516.1; -; Genomic_DNA.
DR EMBL; CP013149; APD01517.1; -; Genomic_DNA.
DR EMBL; CP028977; AWI40862.1; -; Genomic_DNA.
DR EMBL; AP018405; BBA83096.1; -; Genomic_DNA.
DR EMBL; LUXM01000033; KZU94018.1; -; Genomic_DNA.
DR EMBL; MCOL01000001; ODO62100.1; -; Genomic_DNA.
DR EMBL; CP028334; QHM38023.1; -; Genomic_DNA.
DR EMBL; CP028241; QHM48243.1; -; Genomic_DNA.
DR RefSeq; WP_003641531.1; NZ_WYDR01000002.1.
DR GeneID; 77215658; -.
DR KEGG; lpb:SH83_09745; -.
DR PATRIC; fig|1590.142.peg.2090; -.
DR OMA; YDPIFQP; -.
DR Proteomes; UP000076882; Unassembled WGS sequence.
DR Proteomes; UP000093296; Chromosome.
DR Proteomes; UP000094892; Unassembled WGS sequence.
DR Proteomes; UP000183026; Chromosome.
DR Proteomes; UP000244922; Chromosome.
DR Proteomes; UP000269784; Chromosome.
DR Proteomes; UP000464882; Chromosome.
DR Proteomes; UP000465032; Chromosome.
DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00515; HAM1; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR InterPro; IPR020922; dITP/XTP_pyrophosphatase.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR002637; RdgB/HAM1.
DR NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1.
DR PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR SUPFAM; SSF52972; ITPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01405}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01405}.
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 11..16
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
SQ SEQUENCE 202 AA; 21791 MW; C0A70C9BA2043C64 CRC64;
MTKPQTLIIA TNNANKAREF SAMLAPYDIT IKTLADFPNI PEIKENGITF EENATKKATV
VVEATGLPAI ADDSGLMVKA LHGDPGVFSA RYAGDHDDAA NNAKLLANLG GVPEAERTAT
FHTTLVALKP SGEKLVVNGE LAGRILIAPR GDNGFGYDPL FWSSKFQKSL AELTPAQKNQ
ISHRGAALRQ LMTKFDEWWA KA
//