Activities in Family	dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EC 2.4.1.-)
Mechanism	Inverting
Note	Lassak 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 (3591); Uniprot accession (4); PDB accession (12); 3D entries (4); cryst (0)

Bacteria
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D Carbohydrate Ligands Resolution (Å)
NMH_0797 (EarP)		Neisseria meningitidis H44/76	EFV64284.1		5WXI[A,B] 2.00 5WXJ[A,B] 1.85 5WXK[A] 1.80 5XVR[A,B] 1.63
CQR35_05455		Neisseria meningitidis M26263	ATL34055.1		7COX[A,B] 3.00 7F2A[A,B] 2.58 7VCH[A,B] 2.85
dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; PA2852)	2.4.1.-	Pseudomonas aeruginosa PAO1	AAG06240.1	Q9HZZ1	6J7J[A] 1.75 6J7K[A] 2.15 6J7L[A] 1.85 6J7M[A,C] 2.30
dTDP-β-L-Rhap : arginine α-L-rhamnosyltransferase (EarP; PP_1857)	2.4.1.-	Pseudomonas putida KT2440	AAN67476.1	Q88LS1	5NV8[A] 2.29
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