ID 3HAO_COCIM Reviewed; 192 AA. AC Q1E5I0; A0A0D6K9Q5; J3KL46; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 92. 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}; DE AltName: Full=Biosynthesis of nicotinic acid protein 1 {ECO:0000255|HAMAP-Rule:MF_03019}; GN Name=BNA1 {ECO:0000255|HAMAP-Rule:MF_03019}; ORFNames=CIMG_02183; OS Coccidioides immitis (strain RS) (Valley fever fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides. OX NCBI_TaxID=246410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T., RA Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens Coccidioides RT and their relatives."; RL Genome Res. 19:1722-1731(2009). RN [2] RP GENOME REANNOTATION. RC STRAIN=RS; RX PubMed=20516208; DOI=10.1101/gr.103911.109; RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J., RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D., RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A., RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J., RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R., RA Taylor J.W., Rounsley S.D.; RT "Population genomic sequencing of Coccidioides fungi reveals recent RT hybridization and transposon control."; RL Genome Res. 20:938-946(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_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; GG704911; EAS36829.1; -; Genomic_DNA. DR RefSeq; XP_001248412.1; XM_001248411.2. DR AlphaFoldDB; Q1E5I0; -. DR SMR; Q1E5I0; -. DR STRING; 246410.Q1E5I0; -. DR GeneID; 4567554; -. DR KEGG; cim:CIMG_02183; -. DR VEuPathDB; FungiDB:CIMG_02183; -. DR InParanoid; Q1E5I0; -. DR OMA; KPPVGNQ; -. DR OrthoDB; 2907058at2759; -. DR UniPathway; UPA00253; UER00330. DR Proteomes; UP000001261; 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; Reference proteome. FT CHAIN 1..192 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000361986" 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; 21611 MW; 00503228EB6FC03A CRC64; MLAPALNLPK WLEENSHLLQ PPINNYCVYH PSAPATQGYT VMVVGGPNVR TDYHINPTPE FFYQHRGSML LRTVDQSTSP PTFQDIPIHE GSLFLLPANT PHCPVRFADT VGVVLEVPRP ENATDCMRWY CKGCGEIVWE KKFHCTDLGT QVKEVVEEFA ADDEKRKCKA CGSVRSVRYE DGEVVQPPRA PE //