AC MF_01083; DC Protein; auto TR HAMAP; MF_01083; -; 1; level=0 XX Names: glutarate_hydroxylase XX ID GLAH DE RecName: Full=Glutarate 2-hydroxylase; DE Short=G-2-H; DE EC=1.14.11.64; GN Name=glaH; XX CC -!- FUNCTION: Acts as an alpha-ketoglutarate-dependent dioxygenase CC catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate CC (L2HG). Functions in a L-lysine degradation pathway that proceeds via CC cadaverine, glutarate and L-2-hydroxyglutarate. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + glutarate + O2 = (S)-2-hydroxyglutarate + CO2 CC + succinate; Xref=Rhea:RHEA:13821, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:30921; EC=1.14.11.64; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13822; case CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Note=Binds 1 Fe(2+) ion per subunit end case CC -!- PATHWAY: Amino-acid degradation. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the glutarate hydroxylase family. XX DR Pfam; PF08943; CsiD; 1; trigger=no XX KW Dioxygenase KW Oxidoreductase case KW Metal-binding KW Iron end case XX GO GO:0050498; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated GO GO:0019477; P:L-lysine catabolic process case GO GO:0008198; F:ferrous iron binding end case XX FT From: GLAH_ECOLI (P76621) FT BINDING 160 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: H FT BINDING 162 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: D FT BINDING 292 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: H XX Size: 310-325; Related: None; Template: P76621; Scope: Bacteria; Enterobacterales Bacteria; Pseudomonadaceae Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.19 2022/11/19 //