v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase; ) is a dTDP-sugar isomerase enzyme involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria [ ]. RmlC is a dimer, each monomer being formed from two β-sheets arranged in a β-sandwich, where the substrate-binding site is located between the two sheets of both monomers.Other protein families contain domains that share this fold, including glucose-6-phosphate isomerase ( ); germin, a metal-binding protein with oxalate oxidase and superoxide dismutases activities [ ]; auxin-binding protein []; seed storage protein 7S []; acireductone dioxygenase []; as well as three proteins that have metal-binding sites similar to that of germine, namely quercetin 2,3-dioxygenase () [ ], phosphomannose isomerase () [ ] and homogentisate dioxygenase () [ ], the last three sharing a 2-domain fold with storage protein 7s. |
Short Name | RmlC_Cupin_sf |