uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain
Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.
Comment:based on Thermus thermophilus TTHA1623 and on other members of the MBL-fold metallo-hydrolase superfamily with structure and including two metal binding sites
Comment:An acetate, mimicking the hydrolyzed product of an amide or an ester, which are the putative substrates of TTHA1623, was observed 3.0 A away from Fe2 in the metal-binding site of di-iron-bound TTHA1623, resulting in Fe2 bound in a distorted octahedral coordination.
Structure:2ZWR: Thermus thermophilus TTHA1623 binds two Fe ions and an acetate ion; contacts at 4.0A - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",