|Quickview||Gene||Gene Product(s)||Expression||Evolution||On One Page|
UDP-glucuronate dehydrogenase and UDP-ara4N formyltransferase
|Function from GO|
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Involved in the modification of lipid A phosphates with aminoarabinose that is required for polymyxin B and cationic antimicrobial peptide resistance. This bifunctional enzyme catalyzes two steps in lipid A phosphate group modification by aminoarabinose. The C-terminal 345-residues encode the NAD+-dependent dehydrogenase domain that catalyzes the first step in UDP-4-amino-4-deoxy-L-arabinose synthesis and involves successive C4 oxidation and C6 decarboxylation steps. The N-terminal 304-residue domain encodes N-10 formyltetrahydrofolate-dependent UDP-aminoarabinose N-formyltransferase (UDP-formamidoarabinose synthase) that makes the substrate for ArnC: UDP-ara4FN = uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose). ArnA is identical to ssrA-associated factor SAF. basRS regulon.
- Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.