ID 3HAO1_ASPFC Reviewed; 192 AA. AC B0Y9Z9; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 13-SEP-2023, entry version 68. DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase 1 {ECO:0000255|HAMAP-Rule:MF_03019}; DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=3-hydroxyanthranilate oxygenase 1 {ECO:0000255|HAMAP-Rule:MF_03019}; DE Short=3-HAO-1 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase 1 {ECO:0000255|HAMAP-Rule:MF_03019}; DE Short=HAD-1 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=Biosynthesis of nicotinic acid protein 1-1 {ECO:0000255|HAMAP-Rule:MF_03019}; GN Name=bna1-1; ORFNames=AFUB_082850; OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya OS fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=451804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 144.89 / FGSC A1163 / CEA10; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). 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; DS499600; EDP48842.1; -; Genomic_DNA. DR AlphaFoldDB; B0Y9Z9; -. DR SMR; B0Y9Z9; -. DR EnsemblFungi; EDP48842; EDP48842; AFUB_082850. DR VEuPathDB; FungiDB:AFUB_082850; -. DR HOGENOM; CLU_095765_0_0_1; -. DR PhylomeDB; B0Y9Z9; -. DR UniPathway; UPA00253; UER00330. DR Proteomes; UP000001699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Pyridine nucleotide biosynthesis. FT CHAIN 1..192 FT /note="3-hydroxyanthranilate 3,4-dioxygenase 1" FT /id="PRO_0000361976" FT BINDING 50 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 60 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 60 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 102 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 116 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 131 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 134 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 168 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 171 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" SQ SEQUENCE 192 AA; 21705 MW; 148D406C365727F7 CRC64; MLPPALNIPK WLEENSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR TDYHINTTPE FFYQYRGSML LKTVDTSVSP PVFQDIPIHE GSIFLLPANT PHCPVRFKDT VGVVMEQPRP KDAVDTMLWF CKKCGEVVWE KRFVCTDLGT QVKEVVEEFA ADQEKRTCKA CGTIAETRYQ EGEVVQPPRF LE //