ID   3HAO_XANC5              Reviewed;         176 AA.
AC   Q3BV37;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=XCV1645;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O.,
RA   Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A.,
RA   Bonas U., Bartels D., Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant
RT   pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed
RT   by the complete genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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.
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DR   EMBL; AM039952; CAJ23322.1; -; Genomic_DNA.
DR   RefSeq; YP_363376.1; -.
DR   GeneID; 3731279; -.
DR   GenomeReviews; AM039952_GR; XCV1645.
DR   KEGG; xcv:XCV1645; -.
DR   NMPDR; fig|316273.3.peg.1708; -.
DR   HOGENOM; Q3BV37; -.
DR   OMA; Q3BV37; RHSPQRP.
DR   BioCyc; XCAM316273:XCV1645-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    176       3-hydroxyanthranilate 3,4-dioxygenase.
FT                                /FTId=PRO_0000245480.
FT   METAL        48     48       Iron 1; catalytic (By similarity).
FT   METAL        54     54       Iron 1; catalytic (By similarity).
FT   METAL        92     92       Iron 1; catalytic (By similarity).
FT   METAL       121    121       Iron 2 (By similarity).
FT   METAL       124    124       Iron 2 (By similarity).
FT   METAL       158    158       Iron 2 (By similarity).
FT   METAL       161    161       Iron 2 (By similarity).
FT   BINDING      44     44       Dioxygen (By similarity).
FT   BINDING      54     54       Substrate (By similarity).
FT   BINDING      96     96       Substrate (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
SQ   SEQUENCE   176 AA;  20210 MW;  F9638C9EA4618289 CRC64;
     MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMVVGG PNARTDYHYD EGPEWFFQLE
     GEMVLKVQDE GVARDIPIRA GEVFLLPPKV PHSPQRAAGS IGLVIERERL PNEQDGLQWY
     CPQCNHKLYE AMFPLKNIET DFPPVFDRFY RSLALRTCSQ CGHLHPAPER YATVED
//