ID 3HAO_BURL3 Reviewed; 174 AA. AC Q39LI1; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 24-JAN-2024, entry version 101. 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=Bcep18194_C7641; OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / OS R18194 / 383). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 3 of Burkholderia sp. 383."; RL Submitted (OCT-2005) 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_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 -!- SEQUENCE CAUTION: CC Sequence=ABB06685.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000150; ABB06685.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_041492683.1; NC_007509.1. DR AlphaFoldDB; Q39LI1; -. DR SMR; Q39LI1; -. DR GeneID; 45092989; -. DR KEGG; bur:Bcep18194_C7641; -. DR PATRIC; fig|482957.22.peg.8257; -. DR HOGENOM; CLU_095765_0_0_4; -. DR UniPathway; UPA00253; UER00330. DR Proteomes; UP000002705; Chromosome 3. 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..174 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000245474" FT BINDING 47 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 51 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 57 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 57 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 95 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 99 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 110 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 125 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 128 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 162 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" FT BINDING 165 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00825" SQ SEQUENCE 174 AA; 20048 MW; FB19D9C29561A99B CRC64; MLKYGTPFNF SRWIDEHAHL LKPPVGNQQV WQDSDFIVTV VGGPNHRTDY HDDPFEEFFY QLRGNAYLHL WIDGKRERVD LKEGDMFLLP PHVRHSPQRP EAGSACLVIE RQRPAGVVDG FEWYCDACGH LVHRVEVQLK SIVDDLPPLF DAFYASDTLR RCAHCGHMHP GKAT //