LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This domain is found at the C terminus of D-galactarate dehydratase (GarD, ) [ ] and altronate dehydratase () [ ]. When purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn 2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn 2+appears to be part of the enzyme active centre, but the function of the single bound Fe 2+ion is unknown. The hydratase has no Fe-S core [ ]. In the crystal structure, GarD forms dimers, each monomer consisting of three domains: the N-terminal β-clip SAF domain connected by a long linker to the second domain which contains three parallel β-strands surrounded by three α-helices and that serves as a dimerisation interface between monomers, and a C-terminal α/β domain with a novel topology resembling a Rossmann fold, with an unusual helix crossover []. This entry represents the second and C-terminal domains, the latter is the core of the protein and may have a catalytic metal binding site [].This domain is also found in (2R)-sulfolactate sulfo-lyase subunit beta (suyB) ( ) from Chromohalobacter salexigens [ ]. |
| Short Name | Gal/Altron_deHydtase_C |
