ID   NUDJ_ECO24              Reviewed;         153 AA.
AC   A7ZKS4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Phosphatase NudJ;
DE            EC=3.6.1.-;
GN   Name=nudJ; OrderedLocusNames=EcE24377A_1297;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudJ subfamily.
CC       {ECO:0000305}.
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; CP000800; ABV17941.1; -; Genomic_DNA.
DR   RefSeq; WP_000476093.1; NC_009801.1.
DR   AlphaFoldDB; A7ZKS4; -.
DR   SMR; A7ZKS4; -.
DR   EnsemblBacteria; ABV17941; ABV17941; EcE24377A_1297.
DR   GeneID; 66670599; -.
DR   KEGG; ecw:EcE24377A_1297; -.
DR   HOGENOM; CLU_037162_6_1_6; -.
DR   OMA; QPAGHLD; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0017110; F:nucleoside-diphosphatase activity; IEA:InterPro.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0004787; F:thiamine-diphosphatase activity; IEA:InterPro.
DR   CDD; cd03675; Nudix_Hydrolase_2; 1.
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   InterPro; IPR033713; NudJ.
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   Hydrolase; Magnesium.
FT   CHAIN           1..153
FT                   /note="Phosphatase NudJ"
FT                   /id="PRO_0000342641"
FT   DOMAIN          3..131
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           36..57
FT                   /note="Nudix box"
SQ   SEQUENCE   153 AA;  17433 MW;  BDB7423E97D6735A CRC64;
     MFKPHVTVAC VVHAEGKFLV VEETINGKAL WNQPAGHLEA DETLVEAAAR ELWEETGISA
     QPQHFIRMHQ WIAPDKTPFL RFLFAIELEQ ICPTQPHDSD IDCCRWVSAE EILQASNLRS
     PLVAESIRCY QSGQRYPLEM IGDFNWPFTK GVI