NUDI_SALTY
ID NUDI_SALTY Reviewed; 141 AA.
AC Q8ZNF5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Nucleoside triphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=Nucleotide diphosphatase NudI {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=Pyrimidine deoxynucleoside triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=dCTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.12 {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=dTTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01846};
DE AltName: Full=dUTP diphosphatase {ECO:0000255|HAMAP-Rule:MF_01846};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_01846};
GN Name=nudI {ECO:0000255|HAMAP-Rule:MF_01846}; OrderedLocusNames=STM2295;
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a
CC preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and
CC dCTP). {ECO:0000255|HAMAP-Rule:MF_01846}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01846};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01846}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01846}.
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DR EMBL; AE006468; AAL21196.1; -; Genomic_DNA.
DR RefSeq; NP_461237.1; NC_003197.2.
DR RefSeq; WP_001249900.1; NC_003197.2.
DR PDB; 3N77; X-ray; 1.86 A; A/B=1-141.
DR PDB; 3OGA; X-ray; 1.75 A; A/B=1-141.
DR PDBsum; 3N77; -.
DR PDBsum; 3OGA; -.
DR AlphaFoldDB; Q8ZNF5; -.
DR SMR; Q8ZNF5; -.
DR STRING; 99287.STM2295; -.
DR PaxDb; Q8ZNF5; -.
DR EnsemblBacteria; AAL21196; AAL21196; STM2295.
DR GeneID; 1253817; -.
DR KEGG; stm:STM2295; -.
DR PATRIC; fig|99287.12.peg.2429; -.
DR HOGENOM; CLU_037162_31_0_6; -.
DR OMA; RTTKWRG; -.
DR PhylomeDB; Q8ZNF5; -.
DR BioCyc; SENT99287:STM2295-MON; -.
DR EvolutionaryTrace; Q8ZNF5; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047840; F:dCTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR HAMAP; MF_01846; Nudix_NudI; 1.
DR InterPro; IPR023781; Nucleoside_triphosphatase_NudI.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..141
FT /note="Nucleoside triphosphatase NudI"
FT /id="PRO_0000342140"
FT DOMAIN 1..141
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01846"
FT MOTIF 38..59
FT /note="Nudix box"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3OGA"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3OGA"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:3N77"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3OGA"
FT STRAND 64..80
FT /evidence="ECO:0007829|PDB:3OGA"
FT STRAND 86..101
FT /evidence="ECO:0007829|PDB:3OGA"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3OGA"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:3OGA"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:3OGA"
SQ SEQUENCE 141 AA; 16302 MW; 21FF9F381C4B2AA7 CRC64;
MRQRTIVCPL IQNDGCYLLC KMADNRGVFP GQWALSGGGV EPGERIEEAL RREIREELGE
QLILSDITPW TFRDDIRIKT YADGRQEEIY MIYLIFDCVS ANRDICINDE FQDYAWVKPE
ELALYDLNVA TRHTLALKGL L
