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Database: UniProt
Entry: C2QS54_BACCE
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ID   C2QS54_BACCE            Unreviewed;       179 AA.
AC   C2QS54;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   11-JUN-2014, entry version 29.
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){EA2}.
FT   METAL        57     57       Iron 1; catalytic (By similarity){EA2}.
FT   METAL        96     96       Iron 1; catalytic (By similarity){EA2}.
FT   METAL       125    125       Iron 2 (By similarity){EA2}.
FT   METAL       128    128       Iron 2 (By similarity){EA2}.
FT   METAL       162    162       Iron 2 (By similarity){EA2}.
FT   METAL       165    165       Iron 2 (By similarity){EA2}.
FT   BINDING      47     47       Dioxygen (By similarity){EA2}.
FT   BINDING      57     57       Substrate (By similarity){EA2}.
FT   BINDING     100    100       Substrate (By similarity){EA2}.
FT   BINDING     110    110       Substrate (By similarity){EA2}.
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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