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arnA fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947683, updated on 9-Mar-2023

Summary

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Gene symbol
arnA
Gene description
fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
Primary source
ASAP:ABE-0007460
Locus tag
b2255
See related
ECOCYC:G7168
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2248; pmrI; SAF; yfbG
Summary
Involved in the modification of lipid A phosphates with aminoarabinose that is required for polymyxin B and cationic antimicrobial peptide resistance. [More information is available at EcoGene: EG14091]. ArnA is a bifunctional enzyme that acts within a pathway that modifies lipid A phosphates with 4-amino-4-deoxy-L-arabinose (L-Ara4N), which causes increased resistance to polymyxin . [More information is available at EcoCyc: G7168].
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Genomic context

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Sequence:
NC_000913.3 (2368039..2370021)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene UDP-4-amino-4-deoxy-L-arabinose aminotransferase Neighboring gene undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase Neighboring gene putative 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD Neighboring gene lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase Neighboring gene undecaprenyl-phosphate-alpha-L-Ara4N flippase - ArnE subunit Neighboring gene undecaprenyl-phosphate-alpha-L-Ara4N flippase - ArnF subunit Neighboring gene signal transduction protein PmrD

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N. Genthe NA, et al. Protein Sci, 2016 Aug. PMID 27171345, Free PMC Article
  2. The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity. Fischer U, et al. Acta Crystallogr D Biol Crystallogr, 2015 Mar. PMID 25760615
  3. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Gatzeva-Topalova PZ, et al. Structure, 2005 Jun. PMID 15939024, Free PMC Article
  4. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. Williams GJ, et al. J Biol Chem, 2005 Jun 17. PMID 15809294, Free PMC Article
  5. Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Gatzeva-Topalova PZ, et al. Biochemistry, 2005 Apr 12. PMID 15807526, Free PMC Article

See all (26) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N has been presented.
    Title: Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N.
  2. the discovered conformational changes provide a mechanistic explanation for the strong cooperative effect recently reported for the ArnA dehydrogenase function.
    Title: The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity.
  3. N-terminus verified by Edman degradation on complete protein
    Title: Protein factors associated with the SsrA.SmpB tagging and ribosome rescue complex.
  4. analysis of ArnA domains involved in 4-amino-4-deoxy-L-arabinose biosynthesis
    Title: Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by GO

Function Evidence Code Pubs
enables NAD+ binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables UDP-glucuronate decarboxylase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables UDP-glucuronic acid dehydrogenase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables UDP-glucuronic acid dehydrogenase activity IEA
Inferred from Electronic Annotation
more info
  
enables carboxy-lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables hydroxymethyl-, formyl- and related transferase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in UDP-D-xylose biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
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 lipid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lipopolysaccharide biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in response to antibiotic IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within response to antibiotic IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
part_of protein-containing complex IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
NP_416758.1

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
    2368039..2370021
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416758.1 fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416758.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    P77398
    Conserved Domains (1) summary
    PRK08125
    Location:1 → 660
    PRK08125; bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases