AC MF_03019; DC Protein; auto c? TR HAMAP; MF_00825; -; 1; level=0 XX Names: 3_HAO_euk XX ID 3HAO case DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase; DE EC=1.13.11.6; DE AltName: Full=3-hydroxyanthranilate oxygenase; DE Short=3-HAO; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase; DE Short=HAD; DE AltName: Full=Biosynthesis of nicotinic acid protein 1; else DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase; DE EC=1.13.11.6; DE AltName: Full=3-hydroxyanthranilate oxygenase; DE Short=3-HAO; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase; DE Short=HAD; end case case GN Name=HAAO; else case GN Name=BNA1; end case XX CC -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate CC to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes CC to quinolinate. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate CC 6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6; case or CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; end case CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 3/3. case CC -!- SUBUNIT: Monomer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 3-HAO family. XX DR Pfam; PF06052; 3-HAO; 1; trigger=no DR NCBIfam; TIGR03037; Anthran_nbaC; 1; trigger=no XX KW Dioxygenase KW Oxidoreductase KW Pyridine nucleotide biosynthesis case KW Cytoplasm end case case or KW Iron end case case or or KW Metal-binding end case XX GO GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity GO GO:0008198; F:ferrous iron binding GO GO:0006569; P:tryptophan catabolic process GO GO:0019805; P:quinolinate biosynthetic process GO GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan GO GO:0043420; P:anthranilate metabolic process case GO GO:0005737; C:cytoplasm end case XX FT From: 3HAO_BOVIN (Q0VCA8) case FT REGION Nter..160 FT /note="Domain A (catalytic)" FT REGION 161..177 FT /note="Linker" FT REGION 178..Cter FT /note="Domain B" FT BINDING 47 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 53 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: E FT BINDING 91 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 43 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT Condition: R FT BINDING 53 FT /ligand="substrate" FT Condition: E FT BINDING 95 FT /ligand="substrate" FT Condition: R FT BINDING 105 FT /ligand="substrate" FT Condition: E end case FT From: 3HAO_YEAST (P47096) case FT BINDING 49 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 55 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 2; Condition: E FT BINDING 97 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 126 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 3; Condition: C FT BINDING 129 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 3; Condition: C FT BINDING 163 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 3; Condition: C FT BINDING 166 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 3; Condition: C FT BINDING 45 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT Condition: R FT BINDING 55 FT /ligand="substrate" FT Condition: E FT BINDING 101 FT /ligand="substrate" FT Condition: R FT BINDING 111 FT /ligand="substrate" FT Condition: E end case XX Size: 160-288; Related: None; Template: Q0VCA8; Q78JT3; Q54S02; P46952; P47096; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in ASPCL, ASPFC, ASPFU, ASPOR Plasmid: None Comments: None XX # Revision 1.15 2023/06/01 //