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   16-JUN-2009, entry version 27.
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=XC_2679;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA   Fang R., 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-
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; CP000050; AAY49728.1; -; Genomic_DNA.
DR   RefSeq; YP_243748.1; -.
DR   GeneID; 3381213; -.
DR   GenomeReviews; CP000050_GR; XC_2679.
DR   KEGG; xcb:XC_2679; -.
DR   HOGENOM; Q4UT95; -.
DR   OMA; Q4UT95; RHSPQRP.
DR   BioCyc; XCAM314565:XC_2679-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_0000245481.
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;  20128 MW;  3C2FDD218C8458D4 CRC64;
     MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE
     GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY
     CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA
//