ID 3HAO_XANC8 Reviewed; 176 AA. AC Q4UT95; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 97. 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=XC_2679; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8004; RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R., RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). 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; CP000050; AAY49728.1; -; Genomic_DNA. DR RefSeq; WP_011036739.1; NC_007086.1. DR AlphaFoldDB; Q4UT95; -. DR SMR; Q4UT95; -. DR KEGG; xcb:XC_2679; -. DR HOGENOM; CLU_095765_0_0_6; -. DR UniPathway; UPA00253; UER00330. DR Proteomes; UP000000420; Chromosome. 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..176 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000245481" FT BINDING 44 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 48 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 54 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 54 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 92 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 96 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 121 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 124 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 158 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 161 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" SQ SEQUENCE 176 AA; 20128 MW; 3C2FDD218C8458D4 CRC64; MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA //