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IPR011051 is a RmlC-like cupin domain superfamily.
RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase; [ec:5.1.3.13]) is a dTDP-sugar isomerase enzyme involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria [[PMID:10802738]]. 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 ([ec:5.3.1.9]); germin, a metal-binding protein with oxalate oxidase and superoxide dismutases activities [[PMID:11062559]]; auxin-binding protein [[PMID:12065401]]; seed storage protein 7S [[PMID:11124907]]; acireductone dioxygenase [[PMID:12402029]]; as well as three proteins that have metal-binding sites similar to that of germine, namely quercetin 2,3-dioxygenase ([ec:1.13.11.24]) [[PMID:11839311]], phosphomannose isomerase ([ec:5.3.1.8]) [[PMID:8612079]] and homogentisate dioxygenase ([ec:1.13.11.5]) [[PMID:10876237]], the last three sharing a 2-domain fold with storage protein 7s.
This description is obtained from EB-eye REST.