NUDJ_ECOK1
ID NUDJ_ECOK1 Reviewed; 153 AA.
AC A1AA28;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Phosphatase NudJ;
DE EC=3.6.1.-;
GN Name=nudJ; OrderedLocusNames=Ecok1_10240; ORFNames=APECO1_216;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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}.
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DR EMBL; CP000468; ABJ00518.1; -; Genomic_DNA.
DR RefSeq; WP_000476093.1; NC_008563.1.
DR PDB; 3DKU; X-ray; 2.69 A; A/B/C/D/E/F/G/H=1-153.
DR PDB; 3SHD; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-153.
DR PDBsum; 3DKU; -.
DR PDBsum; 3SHD; -.
DR AlphaFoldDB; A1AA28; -.
DR SMR; A1AA28; -.
DR EnsemblBacteria; ABJ00518; ABJ00518; APECO1_216.
DR GeneID; 66670599; -.
DR KEGG; ecv:APECO1_216; -.
DR HOGENOM; CLU_037162_6_1_6; -.
DR OMA; QPAGHLD; -.
DR EvolutionaryTrace; A1AA28; -.
DR Proteomes; UP000008216; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium.
FT CHAIN 1..153
FT /note="Phosphatase NudJ"
FT /id="PRO_0000342642"
FT DOMAIN 3..131
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 36..57
FT /note="Nudix box"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3SHD"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3SHD"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3SHD"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:3SHD"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:3SHD"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3SHD"
SQ SEQUENCE 153 AA; 17433 MW; BDB7423E97D6735A CRC64;
MFKPHVTVAC VVHAEGKFLV VEETINGKAL WNQPAGHLEA DETLVEAAAR ELWEETGISA
QPQHFIRMHQ WIAPDKTPFL RFLFAIELEQ ICPTQPHDSD IDCCRWVSAE EILQASNLRS
PLVAESIRCY QSGQRYPLEM IGDFNWPFTK GVI