| Description | This entry represents the decarboxylase domain of ArnA. This domain can also be found in plant UDP-D-apiose/UDP-D-xylose synthases, such as AXS1/2 from Arabidopsis thaliana. AXS1 catalyses the conversion of UDP-D-glucuronate to a mixture of UDP-D-apiose and UDP-D-xylose [ ].ArnA is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyses the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (α/β folding pattern with a central β-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif [ , , ]. | Name | Bifunctional polymyxin resistance protein ArnA-like, extended (e) SDRs |
| Short Name | Arna-like_SDR_e | Type | Domain |
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