ID D8A5K8_ECOMS Unreviewed; 120 AA. AC D8A5K8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-SEP-2017, entry version 40. DE RecName: Full=Nucleoside triphosphatase NudI {ECO:0000256|HAMAP-Rule:MF_01846}; DE EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01846}; DE AltName: Full=Nucleotide diphosphatase NudI {ECO:0000256|HAMAP-Rule:MF_01846}; DE AltName: Full=Pyrimidine deoxynucleoside triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846}; DE AltName: Full=dCTP diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846}; DE EC=3.6.1.12 {ECO:0000256|HAMAP-Rule:MF_01846}; DE AltName: Full=dTTP diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846}; DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01846}; DE AltName: Full=dUTP diphosphatase {ECO:0000256|HAMAP-Rule:MF_01846}; DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_01846}; GN Name=nudI {ECO:0000256|HAMAP-Rule:MF_01846, GN ECO:0000313|EMBL:EFK21550.1}; GN ORFNames=HMPREF9530_01802 {ECO:0000313|EMBL:EFK21550.1}; OS Escherichia coli (strain MS 21-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK21550.1, ECO:0000313|Proteomes:UP000005688}; RN [1] {ECO:0000313|EMBL:EFK21550.1, ECO:0000313|Proteomes:UP000005688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK21550.1, RC ECO:0000313|Proteomes:UP000005688}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, CC with a preference for pyrimidine deoxynucleoside triphosphates CC (dUTP, dTTP and dCTP). {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- CATALYTIC ACTIVITY: dCTP + H(2)O = dCMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- CATALYTIC ACTIVITY: dTTP + H(2)O = dTMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01846}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01846}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK21550.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ADTR01000165; EFK21550.1; -; Genomic_DNA. DR ProteinModelPortal; D8A5K8; -. DR EnsemblBacteria; EFK21550; EFK21550; HMPREF9530_01802. DR Proteomes; UP000005688; Unassembled WGS sequence. DR GO; GO:0047840; F:dCTP 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; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005688}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01846, KW ECO:0000256|RuleBase:RU003476, ECO:0000256|SAAS:SAAS00636473, KW ECO:0000313|EMBL:EFK21550.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01846}. FT DOMAIN 1 120 Nudix hydrolase. {ECO:0000259|PROSITE: FT PS51462}. FT MOTIF 17 38 Nudix box. {ECO:0000256|HAMAP-Rule: FT MF_01846}. SQ SEQUENCE 120 AA; 13925 MW; 0239D7C72F84AB84 CRC64; MADDRGVFPG QWALSGGGVE PGERIEEALR REIREELGEQ LLLTEITPWT FSDDIRTKTY ADGRKEEIYM IYLIFDCVSA NREVKINEEF QDYAWVKPED LAHYDLNVAT RKTLRLKGLL //