RmlC-like jelly roll fold <p>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; <db_xref db="EC" dbkey="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 [<cite idref="PUB00009949"/>].</p><p>Other protein families contain domains that share this jelly roll fold, including glucose-6-phosphate isomerase (<db_xref db="EC" dbkey="5.3.1.9"/>); germin, a metal-binding protein with oxalate oxidase and superoxide dismutases activities [<cite idref="PUB00014173"/>]; auxin-binding protein [<cite idref="PUB00014174"/>]; seed storage protein 7S [<cite idref="PUB00014175"/>]; acireductone dioxygenase [<cite idref="PUB00014176"/>]; as well as three proteins that have metal-binding sites similar to that of germine, namely quercetin 2,3-dioxygenase (<db_xref db="EC" dbkey="1.13.11.24"/>) [<cite idref="PUB00014177"/>], phosphomannose isomerase (<db_xref db="EC" dbkey="5.3.1.8"/>) [<cite idref="PUB00003929"/>] and homogentisate dioxygenase (<db_xref db="EC" dbkey="1.13.11.5"/>) [<cite idref="PUB00009903"/>], the last three sharing a 2-domain fold with storage protein 7s.</p><p>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 [<cite idref="PUB00034471"/>], and the CnbD (cyclic nucleotide binding domain) of the HCN cation channel in which cAMP binding modulates gating of the channel [<cite idref="PUB00034472"/>].</p>