Vicinal oxygen chelate (VOC), core domain

Definition

This entry represents the core domain in Vicinal oxygen chelate (VOC) proteins. The core domain has topological symmetry, being comprised of two β-α-β-β-β units that form an incompletely closed barrel of β-sheet about the metal ion PMID:21820381. This domain mediates the reactions via its structure and protein-chelating residues that secure and localise a metal ion. The vicinal oxygen chelate (VOC) family of enzymes is a diverse group of proteins found across all domains of life, including bacteria, archaea, and eukarya. These enzymes catalyse a wide range of chemical reactions through a common mechanistic feature: bidentate coordination to a divalent metal centre via vicinal oxygen atoms in the substrate, intermediate, or transition state PMID:35415958. The widespread presence of VOC enzymes across all domains of life highlights their evolutionary significance and critical roles in diverse metabolic pathways and cellular functions PMID:28536594. Some members of this family include: Bacillus thuringiensis, Metallothiol transferase FosB [swissprot:A0RD31] Caenorhabditis elegans, 4-hydroxyphenylpyruvate dioxygenase [swissprot:Q22633] Arabidopsis thaliana, Lactoylglutathione lyase [swissprot:Q8H0V3] Homo sapiens, Glyoxalase domain-containing protein 5 [swissprot:A6NK44].

6 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (6 proteins: gene, accession, name)

• GLO1
• GLOD4
• GLOD5
• HPD
• HPDL
• MCEE