ID   3HAO_PSEFL              Reviewed;         185 AA.
AC   Q83V26;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   20-JAN-2009, entry version 30.
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=nbaC;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION,
RP   COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, AND MUTAGENESIS OF
RP   HIS-52 AND HIS-96.
RC   STRAIN=KU-7;
RX   MEDLINE=22507682; PubMed=12620844;
RX   DOI=10.1128/AEM.69.3.1564-1572.2003;
RA   Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K.;
RT   "Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-
RT   dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
RT   in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens
RT   strain KU-7.";
RL   Appl. Environ. Microbiol. 69:1564-1572(2003).
CC   -!- FUNCTION: Catalyzes the oxidative ring opening of 3-
CC       hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde,
CC       which spontaneously cyclizes to quinolinate.
CC   -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3-
CC       carboxymuconate semialdehyde.
CC   -!- COFACTOR: Binds 2 Fe(2+) ions per subunit (Probable).
CC   -!- ENZYME REGULATION: Inhibited by Zn(2+), Cu(2+) and Cd(2+).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the 3-HAO family.
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DR   EMBL; AB088043; BAC65311.1; -; Genomic_DNA.
DR   SMR; Q83V26; 2-175.
DR   BioCyc; MetaCyc:MON-13359; -.
DR   BRENDA; 1.13.11.6; 329.
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   1: Evidence at protein level;
KW   Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN         1    185       3-hydroxyanthranilate 3,4-dioxygenase.
FT                                /FTId=PRO_0000245472.
FT   METAL        52     52       Iron 1; catalytic (Probable).
FT   METAL        58     58       Iron 1; catalytic (By similarity).
FT   METAL        96     96       Iron 1; catalytic (Probable).
FT   METAL       126    126       Iron 2 (By similarity).
FT   METAL       129    129       Iron 2 (By similarity).
FT   METAL       163    163       Iron 2 (By similarity).
FT   METAL       166    166       Iron 2 (By similarity).
FT   BINDING      48     48       Dioxygen (By similarity).
FT   BINDING      58     58       Substrate (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     111    111       Substrate (By similarity).
FT   MUTAGEN      52     52       H->A: Loss of activity.
FT   MUTAGEN      96     96       H->A: Loss of activity.
SQ   SEQUENCE   185 AA;  21245 MW;  AC932875CC9D3D7D CRC64;
     MMFTFGKPLN FQRWLDDHSD LLRPPVGNQQ VWQDSDFIVT VVGGPNFRTD FHDDPMEEFF
     YQFKGNAYLN IMDRGQMDRV ELKEGDIFLL PPHLRHSPQR PEAGSRCLVI ERQRPKGMLD
     GFEWYCLSCN GLVYRVDVQL NSIVTDLPPL FDIFYGNVGL RKCPQCGQVH PGKAAIEAVA
     RGDQP
//