ID 3HAO_CUPPJ Reviewed; 189 AA. AC Q46PT7; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 111. DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825}; DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_00825}; DE AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_00825}; DE Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_00825}; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825}; DE Short=HAD {ECO:0000255|HAMAP-Rule:MF_00825}; GN Name=nbaC {ECO:0000255|HAMAP-Rule:MF_00825}; GN OrderedLocusNames=Reut_B5502; OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator OS (strain JMP 134)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=264198; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JMP134 / LMG 1197; RX PubMed=20339589; DOI=10.1371/journal.pone.0009729; RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J., RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B., RA Kyrpides N.C.; RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a RT versatile pollutant degrader."; RL PLoS ONE 5:E9729-E9729(2010). CC -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate CC to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes CC to quinolinate. {ECO:0000255|HAMAP-Rule:MF_00825}. 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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00825}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00825}; CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00825}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00825}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00825}. CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP- CC Rule:MF_00825}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000091; AAZ64847.1; -; Genomic_DNA. DR AlphaFoldDB; Q46PT7; -. DR SMR; Q46PT7; -. DR STRING; 264198.Reut_B5502; -. DR KEGG; reu:Reut_B5502; -. DR eggNOG; COG1917; Bacteria. DR HOGENOM; CLU_095765_0_0_4; -. DR OrthoDB; 5002379at2; -. DR UniPathway; UPA00253; UER00330. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule. DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule. DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd06123; cupin_HAO; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR HAMAP; MF_00825; 3_HAO; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR NCBIfam; TIGR03037; anthran_nbaC; 1. DR PANTHER; PTHR15497; 3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE; 1. DR PANTHER; PTHR15497:SF1; 3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE; 1. DR Pfam; PF06052; 3-HAO; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 3: Inferred from homology; KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Pyridine nucleotide biosynthesis. FT CHAIN 1..189 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000245476" FT BINDING 49 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 53 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 59 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 97 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 101 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 112 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 165 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 168 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" SQ SEQUENCE 189 AA; 21938 MW; F3EE0A8DCEEEB74E CRC64; MFDLKYGRPL NFKRWLDDHA DKLKPPVGNQ QIWQDSDMMV TVVGGPNERS DFHDDPIEEL FYQFKGNAYL LLWEDGRYER VDLREGDMLL LPPHTLHSPQ RPEADSRCLV VERKRPQGQN DAFQWSCASC GTIVQRHEVT LQSIVADLPP LYEKFYASSE DARRCPGCGE IHPGRDFQAW HRTLARHSS //