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 (1554); Uniprot accession (0); PDB accession (5); 3D entries (2); cryst (0)
unclassified
Protein Name EC#OrganismGenBank UniprotPDB/3D
 E0Z06_08285 (EarP)   Rheinheimera sp. D18 QBL09505.1    
 E1956_07980 (EarP)   Paraburkholderia sp. 7MH5 QBQ97121.1    
 W01_11490   Candidatus Nitrotoga sp. AM1 BBJ23222.1    
 E3Z29_22725 (EarP)   Pseudomonas sp. S150 QBR33135.1    
 EPZ47_08750 (EarP)   Pseudomonas sp. 11K1 QBZ88796.1    
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