ID   3HAO_ASPNC              Reviewed;         189 AA.
AC   A2R8S7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE            EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE            Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE            Short=HAD {ECO:0000255|HAMAP-Rule:MF_03019};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 1 {ECO:0000255|HAMAP-Rule:MF_03019};
GN   Name=bna1; ORFNames=An16g08210;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate
CC       to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes
CC       to quinolinate. {ECO:0000255|HAMAP-Rule:MF_03019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate
CC         6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03019};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03019};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_03019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03019}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC       Rule:MF_03019}.
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DR   EMBL; AM270377; CAK47070.1; -; Genomic_DNA.
DR   RefSeq; XP_001398119.1; XM_001398082.1.
DR   AlphaFoldDB; A2R8S7; -.
DR   SMR; A2R8S7; -.
DR   EnsemblFungi; CAK47070; CAK47070; An16g08210.
DR   GeneID; 4989212; -.
DR   KEGG; ang:An16g08210; -.
DR   VEuPathDB; FungiDB:An16g08210; -.
DR   HOGENOM; CLU_095765_0_0_1; -.
DR   OrthoDB; 2907058at2759; -.
DR   UniPathway; UPA00253; UER00330.
DR   Proteomes; UP000006706; Chromosome 5R.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06123; cupin_HAO; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   HAMAP; MF_00825; 3_HAO; 1.
DR   InterPro; IPR010329; 3hydroanth_dOase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR03037; anthran_nbaC; 1.
DR   PANTHER; PTHR15497; 3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE; 1.
DR   PANTHER; PTHR15497:SF1; 3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE; 1.
DR   Pfam; PF06052; 3-HAO; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..189
FT                   /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT                   /id="PRO_0000361980"
FT   BINDING         50
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         60
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         102
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         131
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         170
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         173
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
SQ   SEQUENCE   189 AA;  21338 MW;  F10A9D82A81A07A9 CRC64;
     MLPPALNIPK WLETNSHLLQ PPVNNYCVYH PSSPATQGYT VMIVGGPNAR TDYHINTTPE
     FFYQYKGSML LRTVDESSTP PTFQDIPIHE GSLFLLPANT PHCPVRFKDT VGVVMEQPRK
     EGAVDAMRWY CRNKDCGKVV WEKRFVCTDL GTQVKQVVEE FAGDEEKRTC KACGVVARSK
     YEEGEVVQP
//