AC MF_00334; DC Protein; auto TR HAMAP; MF_00334; -; 1; level=0 XX Names: Homogentis_dioxygen XX ID HGD DE RecName: Full=Homogentisate 1,2-dioxygenase; DE Short=HGDO; DE EC=1.13.11.5; DE AltName: Full=Homogentisate oxygenase; DE AltName: Full=Homogentisic acid oxidase; DE AltName: Full=Homogentisicase; GN Name=hmgA; XX CC -!- FUNCTION: Involved in the catabolism of homogentisate (2,5- CC dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the CC degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring CC cleavage of the aromatic ring of homogentisate to yield CC maleylacetoacetate. CC -!- CATALYTIC ACTIVITY: CC Reaction=homogentisate + O2 = 4-maleylacetoacetate + H(+); CC Xref=Rhea:RHEA:15449, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16169, ChEBI:CHEBI:17105; EC=1.13.11.5; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 4/6. CC -!- SUBUNIT: Hexamer; dimer of trimers. CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family. XX DR Pfam; PF04209; HgmA; 1; trigger=no DR NCBIfam; TIGR01015; HmgA; 1; trigger=no XX KW Oxidoreductase KW Dioxygenase KW Metal-binding KW Iron KW Phenylalanine catabolism KW Tyrosine catabolism XX GO GO:0004411; F:homogentisate 1,2-dioxygenase activity GO GO:0005506; F:iron ion binding GO GO:0006559; P:L-phenylalanine catabolic process GO GO:0006572; P:tyrosine catabolic process XX FT From: HGD_PSEPK (Q88E47) FT ACT_SITE 288 FT /note="Proton acceptor" FT Condition: H FT BINDING 349 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Condition: H FT BINDING 355 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Condition: E FT BINDING 385 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Condition: H FT BINDING 346 FT /ligand="homogentisate" FT /ligand_id="ChEBI:CHEBI:16169" FT Condition: y FT BINDING 367 FT /ligand="homogentisate" FT /ligand_id="ChEBI:CHEBI:16169" FT Condition: H XX Size: 416-458; Related: None; Template: Q88E47; Q6EMI9; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: in RALN1 Comments: None XX # Revision 1.33 2023/11/28 //