| Primary Identifier | IPR014710 | Type | Homologous_superfamily |
| Short Name | RmlC-like_jellyroll |
| description | RmlC (deoxythymidine diphosphates-4-dehydrorhamnose 3,5-epimerase; ) is a mainly beta class protein with a jelly roll-like topology. It is a dTDP-sugar isomerase enzyme involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria []. This entry represents the domain with the jelly roll-like fold. Other protein families containing this domain include glucose-6-phosphate isomerase (); germin, a metal-binding protein with oxalate oxidase and superoxide dismutases activities []; auxin-binding protein []; seed storage protein 7S []; acireductone dioxygenase []; as well as three proteins that have metal-binding sites similar to that of germine, namely quercetin 2,3-dioxygenase () [], phosphomannose isomerase () []and homogentisate dioxygenase () [], 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 β-roll architecture consisting of eight antiparallel β-strands and three helical segments []. These proteins include CooA, a CO-sensing haem protein that functions as a transcription activator [], and the CnbD (cyclic nucleotide binding domain) of the HCN cation channel in which cAMP binding modulates gating of the channel []. |
