ID   3HAO_BOVIN              Reviewed;         286 AA.
AC   Q0VCA8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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   Name=HAAO;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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: Fe(2+) ion (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3-
CC       dicarboxylate from L-kynurenine: step 3/3.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the 3-HAO family.
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DR   EMBL; BC120265; AAI20266.1; -; mRNA.
DR   IPI; IPI00715376; -.
DR   RefSeq; NP_001068926.1; -.
DR   UniGene; Bt.20241; -.
DR   Ensembl; ENSBTAG00000004674; Bos taurus.
DR   GeneID; 510602; -.
DR   KEGG; bta:510602; -.
DR   HOVERGEN; Q0VCA8; -.
DR   OMA; Q0VCA8; IMFVGGP.
DR   BRENDA; 1.13.11.6; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010329; 3hydroanth_dOase.
DR   InterPro; IPR016700; 3hydroanth_dOase_met.
DR   Pfam; PF06052; 3-HAO; 1.
DR   PIRSF; PIRSF017681; 3hydroanth_dOase_animal; 1.
DR   TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    286       3-hydroxyanthranilate 3,4-dioxygenase.
FT                                /FTId=PRO_0000283033.
FT   METAL        47     47       Iron; catalytic (By similarity).
FT   METAL        53     53       Iron; catalytic (By similarity).
FT   METAL        91     91       Iron; catalytic (By similarity).
FT   BINDING      43     43       Dioxygen (By similarity).
FT   BINDING      53     53       Substrate (By similarity).
FT   BINDING      95     95       Substrate (By similarity).
FT   BINDING     105    105       Substrate (By similarity).
SQ   SEQUENCE   286 AA;  32493 MW;  6887DDB93B861F8E CRC64;
     MERPVRVKAW VEENRGSFLP PVCNKLLHQK QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG
     DMLLRVLERG KHRDVVIRQG EIFLLPAGVP HSPQRFANTV GLVIERRRLK TELDGLRYYV
     GDTTDVLFEK WFYCEDLGTQ LAPIIQEFFS SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP
     MCLEAWLDGH RKELQAGTPL SLFGDTYESQ VMVHGQGSSE GLRRDVDVWL WQLEGSSVVT
     MEGQRLSLTL DDSLLVPAGT LYGWERGQGS VALSVTQDPA CKKSLG
//