Prolyl 4-hydroxylase alpha subunit, Fe(2+) 2OG dioxygenase domain
IPR044862
Definition
This entry represents the Fe(2) 2-oxoglutarate dioxygenase domain found in prolyl 4-hydroxylase alpha subunit 1/2/3 from animals and related proteins such as PKHD-type hydroxylase YbiX from bacteria. The iron 2OG dioxygenase domain has a conserved β-barrel structure PMID:16782814, which forms a double-stranded β-helix core fold that forms the predominant class of the cupin superfamily ('cupa' means a small barrel in Latin) PMID:14697267. Two histidines and an aspartate residue catalytically bind a metal ion, in general iron but in some cases another metal, directly involved in catalysis. A conserved arginine or lysine residue further near the C-terminal part acts as the basic residue that interacts with the acidic substrate. Mammalian prolyl 4-hydroxylase alpha catalyses the posttranslational formation of 4-hydroxyproline in -xaa-pro-gly-sequences in collagens and other proteins. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor PMID:11276424.
11 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.
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