ID   3HAO_XANAC              Reviewed;         176 AA.
AC   Q8PM31;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 43.
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=XAC1603;
OS   Xanthomonas axonopodis pv. citri (Citrus canker).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=92829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE011792; AAM36471.1; -; Genomic_DNA.
DR   RefSeq; NP_641935.1; -.
DR   GeneID; 1155674; -.
DR   GenomeReviews; AE008923_GR; XAC1603.
DR   KEGG; xac:XAC1603; -.
DR   NMPDR; fig|190486.1.peg.1579; -.
DR   HOGENOM; Q8PM31; -.
DR   OMA; Q8PM31; RHSPQRP.
DR   BioCyc; XAXO190486:XAC1603-MON; -.
DR   BRENDA; 1.13.11.6; 289771.
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_0000245479.
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;  20155 MW;  FBDAA5A96755F310 CRC64;
     MLTPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMVVGG PNARTDYHYD EGPEWFFQLE
     GEMVLKVQDE GVARDIPIRA GEVFLLPPKV PHSPQRADGS IGLVIERERL PTEQDGLQWY
     CPQCNHKLYE AMFPLKNIET DFPPVFDRFY RSPALRTCSQ CGHLHPAPER YATVEG
//