3HAO_ASPNC
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 03-AUG-2022, entry version 84.
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 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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;
CC Evidence={ECO:0000255|HAMAP-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 PaxDb; A2R8S7; -.
DR EnsemblFungi; CAK47070; CAK47070; An16g08210.
DR GeneID; 4989212; -.
DR KEGG; ang:ANI_1_1110144; -.
DR VEuPathDB; FungiDB:An16g08210; -.
DR HOGENOM; CLU_095765_0_0_1; -.
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; -; 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 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 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
