RmlC-like cupin domain superfamily
IPR011051
Definition
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.
9 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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