ID 3HAO_BACAH Reviewed; 179 AA. AC A0RD64; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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=BALH_1838; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/jb.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). 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 -!- 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; CP000485; ABK85157.1; -; Genomic_DNA. DR RefSeq; WP_000047734.1; NC_008600.1. DR AlphaFoldDB; A0RD64; -. DR SMR; A0RD64; -. DR KEGG; btl:BALH_1838; -. DR HOGENOM; CLU_095765_0_0_9; -. DR UniPathway; UPA00253; UER00330. DR Proteomes; UP000000761; 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..179 FT /note="3-hydroxyanthranilate 3,4-dioxygenase" FT /id="PRO_0000309575" 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 96 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 100 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 179 AA; 20985 MW; 1A5BF15A9B2302AC CRC64; MSKTLQSFNL LKWIDENKEL LKPPVNNKVI WQDSEFIAMI LGGPNRRRDF HVDPSDEFFY QIKGECYVEC ITEEGKREVV TVKEGDVFML PAMVPHSPHR VANTYGLVIE RKRSQGELED FVWFCDECNH EMHRVRVQLS DIEKQVKEAI HSFNSNKEIR ACKNCGHIMP EEVGEWKCE //