NUDI_KLEP7
ID NUDI_KLEP7 Reviewed; 140 AA.
AC A6TBV3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 70.
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};
GN OrderedLocusNames=KPN78578_26130; ORFNames=KPN_02657;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABR78074.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000647; ABR78074.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_009484772.1; NC_009648.1.
DR AlphaFoldDB; A6TBV3; -.
DR SMR; A6TBV3; -.
DR STRING; 272620.KPN_02657; -.
DR PRIDE; A6TBV3; -.
DR EnsemblBacteria; ABR78074; ABR78074; KPN_02657.
DR KEGG; kpn:KPN_02657; -.
DR HOGENOM; CLU_037162_31_0_6; -.
DR Proteomes; UP000000265; Chromosome.
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: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; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..140
FT /note="Nucleoside triphosphatase NudI"
FT /id="PRO_0000342134"
FT DOMAIN 1..140
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01846"
FT MOTIF 38..58
FT /note="Nudix box"
SQ SEQUENCE 140 AA; 16172 MW; 574A06A474FC8451 CRC64;
MRHRTIVCPL IENKGHYLLC KMAADRGVFP GQWALSGGVE PGERIEEALR REIREELGEK
LILTHIAPWC FRDDTRVKTY PDGHQETIYM IYLIFNCVSA NRDVTINEEF DDYAWVKAED
LKNYDLNAAT RVTLSLKGLL
