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Database: UniProt
Entry: C2QS54_BACCE
LinkDB: C2QS54_BACCE
Original site: C2QS54_BACCE 
ID   C2QS54_BACCE            Unreviewed;       179 AA.
AC   C2QS54;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   19-FEB-2014, entry version 28.
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase;
DE            EC=1.13.11.6;
DE   AltName: Full=3-hydroxyanthranilate oxygenase;
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase;
GN   Name=nbaC; ORFNames=bcere0010_18730;
OS   Bacillus cereus ATCC 4342.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=526977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 4342;
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 3/3.
CC   -!- SIMILARITY: Belongs to the 3-HAO family.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; ACLZ01000026; EEK84513.1; -; Genomic_DNA.
DR   ProteinModelPortal; C2QS54; -.
DR   EnsemblBacteria; EEK84513; EEK84513; bcere0010_18730.
DR   PATRIC; 24873493; VBIBacCer13872_1593.
DR   UniPathway; UPA00253; UER00330.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_00825; 3_HAO; 1.
DR   InterPro; IPR010329; 3hydroanth_dOase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin.
DR   PANTHER; PTHR15497; PTHR15497; 1.
DR   Pfam; PF06052; 3-HAO; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
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;  21084 MW;  1A4A10AA8AC192AC CRC64;
     MSKTLQSFNL LKWIDENKEL LKPPVNNKVI WQDSEFIAMI LGGPNRRRDF HVDPSDEFFY
     QIKGECYVEC ITEEGKREVV TVKEGDVFML PAMVPHSPHR VANTYGLVIE RKRNQGELED
     FVWFCDECNH EMHRVRVQLS DIEKQVKEAI HSFNSNKEIR ACKNCGHIMP EEVEEWKCE
//
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