InterPro: IPR014710 RmlC-like jelly roll fold

This entry represents domains with a double-stranded beta-helix jelly roll fold such as that found in RmlC (deoxythimodone diphosphates-4-dehydrorhamnose 3,5-epimerase; EC:5.1.3.13), a dTDP-sugar isomerase enzyme involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria [1].

Other protein families contain domains that share this jelly roll fold, including glucose-6-phosphate isomerase (EC:5.3.1.9); germin, a metal-binding protein with oxalate oxidase and superoxide dismutases activities [2]; auxin-binding protein [3]; seed storage protein 7S [4]; acireductone dioxygenase [5]; 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) [6], phosphomannose isomerase (EC:5.3.1.8) [7] and homogentisate dioxygenase (EC:1.13.11.5) [8], the last three sharing a 2-domain fold with storage protein 7s.

The cAMP-binding domains found in the cAMP receptor protein (CRP) family display a similar double-stranded beta-helix jelly roll fold. These proteins include CooA, a CO-sensing haem protein that functions as a transcription activator [9], and the CnbD (cyclic nucleotide binding domain) of the HCN cation channel in which cAMP binding modulates gating of the channel [10].