ID 3HAO_CAEEL Reviewed; 281 AA. AC Q19341; Q21258; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 2. DT 27-MAR-2024, entry version 158. 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-1; ORFNames=K06A4.5; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-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; Z70755; CAA94787.1; -; Genomic_DNA. DR EMBL; Z70751; CAA94787.1; JOINED; Genomic_DNA. DR PIR; T20743; T20743. DR RefSeq; NP_505450.1; NM_073049.1. DR AlphaFoldDB; Q19341; -. DR SMR; Q19341; -. DR BioGRID; 44367; 5. DR IntAct; Q19341; 5. DR MINT; Q19341; -. DR STRING; 6239.K06A4.5.1; -. DR EPD; Q19341; -. DR PaxDb; 6239-K06A4-5; -. DR PeptideAtlas; Q19341; -. DR EnsemblMetazoa; K06A4.5.1; K06A4.5.1; WBGene00010595. DR EnsemblMetazoa; K06A4.5.2; K06A4.5.2; WBGene00010595. DR GeneID; 179329; -. DR KEGG; cel:CELE_K06A4.5; -. DR UCSC; K06A4.5; c. elegans. DR AGR; WB:WBGene00010595; -. DR WormBase; K06A4.5; CE06109; WBGene00010595; haao-1. DR eggNOG; KOG3995; Eukaryota. DR GeneTree; ENSGT00390000013008; -. DR HOGENOM; CLU_064845_0_0_1; -. DR InParanoid; Q19341; -. DR OMA; NAPYEAR; -. DR OrthoDB; 2907058at2759; -. DR PhylomeDB; Q19341; -. DR Reactome; R-CEL-71240; Tryptophan catabolism. DR UniPathway; UPA00253; UER00330. DR PRO; PR:Q19341; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00010595; Expressed in larva and 2 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule. 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:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. 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; 1. DR World-2DPAGE; 0011:Q19341; -. PE 3: Inferred from homology; KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1..281 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000245470" FT REGION 1..162 FT /note="Domain A (catalytic)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT REGION 163..179 FT /note="Linker" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT REGION 180..281 FT /note="Domain B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 45 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 49 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 55 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 55 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 93 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 97 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" SQ SEQUENCE 281 AA; 32227 MW; E3DD76D60D5930A9 CRC64; MSGVTAIEIP QWIQDNQEDF VPPVCNKCMF SDQLKVFYVG GPNQRKDFHL EEGEEFFFQR KGDMVLKVIE KGQVRDLVIK QGEMFMLPAR VEHSPQRFSN SIGLVVERER KNTEFDCVRF LVGSSNITLF ERWFYLTDVV KDLPPLIKEF YGSNEFKTGK PGKGTFACNA PYEARWTDLP VPINRKEFIY DHISEVKNGP VRIYGAPEYK TEVMLLGEGS YDLESGTVEL LIWLQENTFA VVEESGFTYA MKSETMVRIK PNTKCLLNVK GGFAITIRMP A //