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   16-JUN-2009, entry version 18.
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=BALH_1838;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   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-
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   -!- SIMILARITY: Belongs to the 3-HAO family.
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DR   EMBL; CP000485; ABK85157.1; -; Genomic_DNA.
DR   RefSeq; YP_894664.1; -.
DR   GeneID; 4545488; -.
DR   GenomeReviews; CP000485_GR; BALH_1838.
DR   KEGG; btl:BALH_1838; -.
DR   NMPDR; fig|412694.5.peg.1824; -.
DR   OMA; A0RD64; RHSPQRP.
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    179       3-hydroxyanthranilate 3,4-dioxygenase.
FT                                /FTId=PRO_0000309575.
FT   METAL        51     51       Iron 1; catalytic (By similarity).
FT   METAL        57     57       Iron 1; catalytic (By similarity).
FT   METAL        96     96       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     100    100       Substrate (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
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
//