ID 3HAO_XANCB Reviewed; 176 AA.
AC B0RUZ7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 29-MAY-2013, entry version 44.
DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase;
DE EC=1.13.11.6;
DE AltName: Full=3-hydroxyanthranilate oxygenase;
DE Short=3-HAO;
DE AltName: Full=3-hydroxyanthranilic acid dioxygenase;
DE Short=HAD;
GN Name=nbaC; OrderedLocusNames=xcc-b100_2705;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J.,
RA Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A.,
RA Niehaus K., Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use
RT for the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the 3-HAO family.
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DR EMBL; AM920689; CAP52066.1; -; Genomic_DNA.
DR RefSeq; YP_001904110.1; NC_010688.1.
DR ProteinModelPortal; B0RUZ7; -.
DR STRING; 509169.xccb100_2705; -.
DR EnsemblBacteria; CAP52066; CAP52066; xcc-b100_2705.
DR GeneID; 6322736; -.
DR KEGG; xca:xccb100_2705; -.
DR PATRIC; 24085325; VBIXanCam108527_2743.
DR eggNOG; NOG77058; -.
DR KO; K00452; -.
DR OMA; HSPQRPE; -.
DR ProtClustDB; PRK13264; -.
DR BioCyc; XCAM509169:GHW4-2765-MONOMER; -.
DR UniPathway; UPA00253; UER00330.
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 Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis.
FT CHAIN 1 176 3-hydroxyanthranilate 3,4-dioxygenase.
FT /FTId=PRO_1000134551.
FT METAL 48 48 Iron 1; catalytic (By similarity).
FT METAL 54 54 Iron 1; catalytic (By similarity).
FT METAL 92 92 Iron 1; catalytic (By similarity).
FT METAL 121 121 Iron 2 (By similarity).
FT METAL 124 124 Iron 2 (By similarity).
FT METAL 158 158 Iron 2 (By similarity).
FT METAL 161 161 Iron 2 (By similarity).
FT BINDING 44 44 Dioxygen (By similarity).
FT BINDING 54 54 Substrate (By similarity).
FT BINDING 96 96 Substrate (By similarity).
FT BINDING 106 106 Substrate (By similarity).
SQ SEQUENCE 176 AA; 20172 MW; 3C3D78418C8458D4 CRC64;
MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE
GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY
CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCMQ CGHVHPAPER YAAIEA
//