U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    arnB UDP-4-amino-4-deoxy-L-arabinose aminotransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947375, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    arnB
    Official Full Name
    UDP-4-amino-4-deoxy-L-arabinose aminotransferase
    Primary source
    ECOCYC:G7166
    Locus tag
    b2253
    See related
    ASAP:ABE-0007456
    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
    ECK2246; pmrH; yfbE
    Summary
    Involved in a lipid A modification required for polymyxin B and cationic antimicrobial peptide resistance. basRS regulon. [More information is available at EcoGene: EG14089]. ArnB is a UDP-L-Ara4O C-4" transaminase that acts in a pathway which modifies lipid A phosphates with 4-amino-4-deoxy-L-arabinose (L-Ara4N), causing increased resistance to polymyxin . [More information is available at EcoCyc: G7166].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (2365910..2367067)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene pyrimidine deoxynucleotide diphosphatase NudI Neighboring gene putative lipopolysaccharide core heptose(II)-phosphate phosphatase Neighboring gene undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase Neighboring gene fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase Neighboring gene putative 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. Noland BW, et al. Structure, 2002 Nov. PMID 12429098
    2. Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli. An aminotransferase (ArnB) that generates UDP-4-deoxyl-L-arabinose. Breazeale SD, et al. J Biol Chem, 2003 Jul 4. PMID 12704196
    3. Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. Breazeale SD, et al. J Biol Chem, 2002 Jan 25. PMID 11706007
    4. A pmrA constitutive mutant sensitizes Escherichia coli to deoxycholic acid. Froelich JM, et al. J Bacteriol, 2006 Feb. PMID 16428424, Free PMC Article
    5. Lipopolysaccharides of polymyxin B-resistant mutants of Escherichia coli are extensively substituted by 2-aminoethyl pyrophosphate and contain aminoarabinose in lipid A. Nummila K, et al. Mol Microbiol, 1995 Apr. PMID 7565089

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

    Go to the top of the page

    General gene information

    Go to the top of the page Help

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables UDP-4-amino-4-deoxy-L-arabinose aminotransferase IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables UDP-4-amino-4-deoxy-L-arabinose aminotransferase IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables pyridoxal phosphate binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables pyridoxal phosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables transaminase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables transaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in lipid A biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid A metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipopolysaccharide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in polysaccharide biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in response to antibiotic IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    UDP-4-amino-4-deoxy-L-arabinose aminotransferase
    NP_416756.6

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      2365910..2367067
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416756.6 UDP-4-amino-4-deoxy-L-arabinose aminotransferase [Escherichia coli str. K-12 substr. MG1655]

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0AAE9R0X3
      Conserved Domains (1) summary
      PRK11658
      Location:7 → 385
      PRK11658; UDP-4-amino-4-deoxy-L-arabinose aminotransferase
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.