ID C2QS54_BACCE Unreviewed; 179 AA.
AC C2QS54;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 29-MAY-2013, entry version 24.
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0043420; P:anthranilate metabolic process; IEA:HAMAP.
DR GO; GO:0034354; P:de novo NAD biosynthetic process from tryptophan; IEA:HAMAP.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:HAMAP.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA: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; RmlC_like_cupin; 1.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 3: Inferred from homology;
KW 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
//
