GlycosylTransferase Family 104

Activities in FamilydTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EC 2.4.1.-)
Mechanism Inverting
NoteLassak et al. identified EarP as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-b-L-rhamnose as donor substrate (PMID=25686373). The results of this study were subsequently confirmed for Pseudomonas aeruginosa (PMID=26060278), Pseudomonas putida (PMID=28951478) and Neisseria meningitidis (PMID=26840407). In 2016, it has been shown for S. oneidensis (PMID=28451135) and P. aeruginosa (PMID=28451332) that the enzyme is an inverting glycosyltransferase, thus mediating the formation of an a-L-rhamnosidic linkage. A structural basis for the arginine glycosylation reaction was provided by Krafczyk, Macosek and coworkers by having solved the crystal structure of the GT-B folding EarP from P. putida and an accompanying biochemical analysis of the enzyme (PMID=28951478).
Statistics GenBank accession (1018); Uniprot accession (0); PDB accession (1); 3D entries (1); cryst (0)
All (1021) Bacteria (1021) Structure (1) Characterized (4)
Bacteria
Protein Name EC#OrganismGenBankUniprot
PDB/3D Carbohydrate Ligands Resolution (Å)
 dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; PP_1857) 2.4.1.- Pseudomonas putida KT2440 SKB80791.1
AAN67476.1
 
5NV8[A] 2.29
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