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 (1885); Uniprot accession (0); PDB accession (9); 3D entries (3); cryst (0)
All (1882) Bacteria (1882) Structure (3) Characterized (4)
Bacteria
Protein Name EC#OrganismGenBank UniprotPDB/3D
  dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; SO_2329) 2.4.1.- Neisseria meningitidis NIID280 BAU19337.1    
 dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; PA2852) 2.4.1.- Pseudomonas aeruginosa PAO1 AAG06240.1   6J7J[A]
6J7K[A]
6J7L[A]
6J7M[A,C]
 dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; PP_1857) 2.4.1.- Pseudomonas putida KT2440 AAN67476.1   5NV8[A]
 dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; SO_2329) 2.4.1.- Shewanella oneidensis MR-1 AAN55363.1    
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