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nudJ phosphatase NudJ [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945689, updated on 3-Dec-2024

Summary

Official Symbol
nudJ
Official Full Name
phosphatase NudJ
Primary source
ECOCYC:G6580
Locus tag
b1134
See related
ASAP:ABE-0003818
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1120; ymfB
Summary
Nudix hydrolase. [More information is available at EcoGene: EG13446]. The nudJ gene product is a member of the Nudix hydrolase superfamily. [More information is available at EcoCyc: G6580].
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Genomic context

Sequence:
NC_000913.3 (1193827..1194288, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene lysogenization regulator Neighboring gene tRNA-specific 2-thiouridylase Neighboring gene 23S rRNA pseudouridine(2457) synthase Neighboring gene isocitrate dehydrogenase

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General protein information

Preferred Names
phosphatase NudJ
NP_415652.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1193827..1194288 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415652.1 phosphatase NudJ [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415652.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A418GAI7
    Conserved Domains (1) summary
    cd03675
    Location:6137
    Nudix_Hydrolase_2; Contains a crystal structure of the Nudix hydrolase from Nitrosomonas europaea, which has an unknown function. In general, members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes ...