ID 3HAO_DANRE Reviewed; 287 AA. AC Q5U3F8; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019}; DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_03019}; DE Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019}; DE Short=HAD {ECO:0000255|HAMAP-Rule:MF_03019}; GN Name=haao; ORFNames=zgc:103585; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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_03019}. 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_03019}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03019}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_03019}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03019}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP- CC Rule:MF_03019}. CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP- CC Rule:MF_03019}. 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; BC085560; AAH85560.1; -; mRNA. DR RefSeq; NP_001007391.1; NM_001007390.1. DR AlphaFoldDB; Q5U3F8; -. DR SMR; Q5U3F8; -. DR STRING; 7955.ENSDARP00000091014; -. DR PaxDb; 7955-ENSDARP00000091014; -. DR GeneID; 492518; -. DR KEGG; dre:492518; -. DR AGR; ZFIN:ZDB-GENE-041114-89; -. DR CTD; 23498; -. DR ZFIN; ZDB-GENE-041114-89; haao. DR eggNOG; KOG3995; Eukaryota. DR InParanoid; Q5U3F8; -. DR OrthoDB; 2907058at2759; -. DR PhylomeDB; Q5U3F8; -. DR Reactome; R-DRE-71240; Tryptophan catabolism. DR UniPathway; UPA00253; UER00330. DR PRO; PR:Q5U3F8; -. DR Proteomes; UP000000437; Chromosome 13. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; ISS:UniProtKB. DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB. DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IBA:GO_Central. DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009435; P:NAD biosynthetic process; ISS:UniProtKB. DR GO; GO:0019805; P:quinolinate biosynthetic process; ISS:UniProtKB. DR GO; GO:0046874; P:quinolinate metabolic process; IBA:GO_Central. 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; IPR016700; 3hydroanth_dOase_met. 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 PIRSF; PIRSF017681; 3hydroanth_dOase_animal; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 2. PE 2: Evidence at transcript level; KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1..287 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000245466" FT REGION 1..163 FT /note="Domain A (catalytic)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT REGION 164..180 FT /note="Linker" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT REGION 181..287 FT /note="Domain B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 46 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 50 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 56 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 94 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" SQ SEQUENCE 287 AA; 33239 MW; A5A2B050B823F038 CRC64; MTNQSLHVNI DKWIAENETS FLPPVCNKLM FFYQLNIMYV GGPNVRKDYH IEEGEELFYQ VRGDMVLKVI ENGKHKDVHI REGEMFLLPA RIPHSPQRQA NTVGLVIERR RLSKETDGLR YFVANSTEVL FERWFYCENL GTQLVPIIKE FMDSKENETG KPDPANPIKP APYPLNTMNV MTPFSFREWV EKQKPVLASG CPVDMFGEQF ETETLLFGSG TSANKRRTDG WIWQLEGLSN VFMNGKEYSL TAGDCLLIFG ETEYKWQRSQ DCVALYVAQD PDRKRPY //