ID 3HAO_BURS3 Reviewed; 174 AA. AC Q39LI1; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 04-NOV-2008, entry version 30. DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase; DE EC=1.13.11.6; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase; DE Short=HAD; DE AltName: Full=3-hydroxyanthranilate oxygenase; DE Short=3-HAO; GN OrderedLocusNames=Bcep18194_C7641; OS Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 OS / NCIB 9086 / R18194)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=269483; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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- CC hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, CC which spontaneously cyclizes to quinolinate (By similarity). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Binds 2 Fe(2+) ions per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the 3-HAO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000150; ABB06685.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_367329.1; -. DR SMR; Q39LI1; 1-173. DR GeneID; 3734508; -. DR GenomeReviews; CP000150_GR; Bcep18194_C7641. DR KEGG; bur:Bcep18194_C7641; -. DR NMPDR; fig|269483.3.peg.4346; -. DR HOGENOM; Q39LI1; -. DR BioCyc; BSP36773:BCEP18194_C7641-MON; -. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:HAMAP. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR Pfam; PF06052; 3-HAO; 1. DR TIGRFAMs; TIGR03037; anthran_nbaC; 1. PE 3: Inferred from homology; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 174 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245474. FT METAL 51 51 Iron 1; catalytic (By similarity). FT METAL 57 57 Iron 1; catalytic (By similarity). FT METAL 95 95 Iron 1; catalytic (By similarity). FT METAL 125 125 Iron 2 (By similarity). FT METAL 128 128 Iron 2 (By similarity). FT METAL 162 162 Iron 2 (By similarity). FT METAL 165 165 Iron 2 (By similarity). FT BINDING 47 47 Dioxygen (By similarity). FT BINDING 57 57 Substrate (By similarity). FT BINDING 99 99 Substrate (By similarity). FT BINDING 110 110 Substrate (By similarity). 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 //