Homologous Superfamily

RmlC-like jelly roll fold (IPR014710)

Short name: RmlC-like_jellyroll

Overlapping entries

«
»

Description

RmlC (deoxythymidine diphosphates-4-dehydrorhamnose 3,5-epimerase; EC:5.1.3.13) 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 [PMID: 10802738]. This entry represents the domain with the jelly roll-like fold.

Other protein families containing this domain include 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.

The cAMP-binding domains found in the cAMP receptor protein (CRP) family display a similar beta-roll architecture consisting of eight antiparallel beta-strands and three helical segments [PMID: 11017196]. These proteins include CooA, a CO-sensing haem protein that functions as a transcription activator [PMID: 10196160], and the CnbD (cyclic nucleotide binding domain) of the HCN cation channel in which cAMP binding modulates gating of the channel [PMID: 16500960].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
GENE3D