ID 3HAO2_ASPFU Reviewed; 188 AA. AC Q4WZC3; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 24-JAN-2024, entry version 104. DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase 2 {ECO:0000255|HAMAP-Rule:MF_03019}; DE EC=1.13.11.6 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=3-hydroxyanthranilate oxygenase 2 {ECO:0000255|HAMAP-Rule:MF_03019}; DE Short=3-HAO-2 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase 2 {ECO:0000255|HAMAP-Rule:MF_03019}; DE Short=HAD-2 {ECO:0000255|HAMAP-Rule:MF_03019}; DE AltName: Full=Biosynthesis of nicotinic acid protein 1-2 {ECO:0000255|HAMAP-Rule:MF_03019}; GN Name=bna1-2; ORFNames=AFUA_2G17450; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=EAL94042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=EAL94042.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000001; EAL94042.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_756080.1; XM_750987.1. DR AlphaFoldDB; Q4WZC3; -. DR SMR; Q4WZC3; -. DR STRING; 330879.Q4WZC3; -. DR GeneID; 3513434; -. DR KEGG; afm:AFUA_2G17450; -. DR eggNOG; KOG3995; Eukaryota. DR HOGENOM; CLU_095765_0_0_1; -. DR InParanoid; Q4WZC3; -. DR OrthoDB; 2907058at2759; -. DR UniPathway; UPA00253; UER00330. DR Proteomes; UP000002530; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule. DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IBA:GO_Central. 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:0046874; P:quinolinate metabolic process; IBA:GO_Central. 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:SF3; 3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE 2; 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..188 FT /note="3-hydroxyanthranilate 3,4-dioxygenase 2" FT /id="PRO_0000361979" FT BINDING 46 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 50 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 70 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 108 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 112 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019" SQ SEQUENCE 188 AA; 22079 MW; 0531413AEF55A832 CRC64; MATLNPLSWV TWLAENEDKL RPPVNNYCLY QGNDFILMAV GGPNERNDYH VNETEVRLQW HQPSETNEQE WFYQVQGDML LRVIENDTFR DIPIKEGEMF LLPGNTPHNP VRYKDTIGLV MERQRPAESR DRLRWYCTKG NHCSPTIIRE EVFHCADLGS QLKPIIERWQ QDEESRRCGE CGCIADPK //