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Database: UniProt/SWISS-PROT
Entry: 3HAO_XANCB
LinkDB: 3HAO_XANCB
Original site: 3HAO_XANCB 
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   26-NOV-2014, entry version 50.
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE            EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_00825};
DE   AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE            Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_00825};
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_00825};
DE            Short=HAD {ECO:0000255|HAMAP-Rule:MF_00825};
GN   Name=nbaC {ECO:0000255|HAMAP-Rule:MF_00825};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_00825}.
CC   -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3-
CC       carboxymuconate semialdehyde. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00825};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00825};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00825}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00825}.
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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; HINQTPE; -.
DR   OrthoDB; EOG6PW234; -.
DR   BioCyc; XCAM509169:GHW4-2765-MONOMER; -.
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   CHAIN         1    176       3-hydroxyanthranilate 3,4-dioxygenase.
FT                                /FTId=PRO_1000134551.
FT   METAL        48     48       Iron 1; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   METAL        54     54       Iron 1; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   METAL        92     92       Iron 1; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   METAL       121    121       Iron 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   METAL       124    124       Iron 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   METAL       158    158       Iron 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   METAL       161    161       Iron 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   BINDING      44     44       Dioxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   BINDING      54     54       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   BINDING      96     96       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
FT   BINDING     106    106       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00825}.
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
//
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