ID A0A7Z2QXS4_9PSED Unreviewed; 148 AA. AC A0A7Z2QXS4; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-MAY-2023, entry version 7. DE RecName: Full=Phosphatase NudJ {ECO:0000256|ARBA:ARBA00015552, ECO:0000256|RuleBase:RU364043}; DE EC=3.6.1.- {ECO:0000256|RuleBase:RU364043}; GN Name=nudJ {ECO:0000256|RuleBase:RU364043}; GN ORFNames=N015_11180 {ECO:0000313|EMBL:QHF02943.1}; OS Pseudomonas asturiensis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1190415 {ECO:0000313|EMBL:QHF02943.1, ECO:0000313|Proteomes:UP000464644}; RN [1] {ECO:0000313|EMBL:QHF02943.1, ECO:0000313|Proteomes:UP000464644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC1524 {ECO:0000313|EMBL:QHF02943.1, RC ECO:0000313|Proteomes:UP000464644}; RX PubMed=24459267; RA Baltrus D.A., Yourstone S., Lind A., Guilbaud C., Sands D.C., Jones C.D., RA Morris C.E., Dangl J.L.; RT "Draft Genome Sequences of a Phylogenetically Diverse Suite of Pseudomonas RT syringae Strains from Multiple Source Populations."; RL Genome Announc. 2:e01195-e01113(2014). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU364043}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, CC ECO:0000256|RuleBase:RU364043}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudJ subfamily. CC {ECO:0000256|ARBA:ARBA00007608, ECO:0000256|RuleBase:RU364043}. 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; CP047265; QHF02943.1; -; Genomic_DNA. DR RefSeq; WP_024685536.1; NZ_CP047265.1. DR AlphaFoldDB; A0A7Z2QXS4; -. DR KEGG; past:N015_11180; -. DR Proteomes; UP000464644; Chromosome. DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro. DR GO; GO:0004787; F:thiamine diphosphate phosphatase activity; IEA:InterPro. DR CDD; cd03675; Nudix_Hydrolase_2; 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR033713; NudJ. DR PANTHER; PTHR43222; NUDIX HYDROLASE 23; 1. DR PANTHER; PTHR43222:SF11; PHOSPHATASE NUDJ; 1. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; Nudix; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364043}; KW Magnesium {ECO:0000256|RuleBase:RU364043}. FT DOMAIN 2..131 FT /note="Nudix hydrolase" FT /evidence="ECO:0000259|PROSITE:PS51462" SQ SEQUENCE 148 AA; 16981 MW; A2A5B011694B7C4A CRC64; MRWQAHVTVA TIVEDQGRFL FVEEIKGGRS VLNQPAGHLD PNESLQRAAV RETLEETGWD VELTSVVGIY LYTAPSNGVT YQRICFAAKA LRHHPDYRLD EGIVGPVWLT RDELLAEQDR WRSELVLRCM DDYLNAEHFS LDLLRDKA //