Domain

RmlC-like cupin domain (IPR011051)

Short name: RmlC_Cupin

Domain relationships

Description

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 beta-sheets arranged in a beta-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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
SUPERFAMILY