ID   3HAO_YEAST              Reviewed;         177 AA.
AC   P47096; D6VWJ8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 196.
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 {ECO:0000255|HAMAP-Rule:MF_03019}; Synonyms=HAD1;
GN   OrderedLocusNames=YJR025C; ORFNames=J1550;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8619316; DOI=10.1002/yea.320111208;
RA   Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J.,
RA   Herbert C.J.;
RT   "The sequence of 24.3 kb from chromosome X reveals five complete open
RT   reading frames, all of which correspond to new genes, and a tandem
RT   insertion of a Ty1 transposon.";
RL   Yeast 11:1179-1186(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=9539135; DOI=10.1016/s0014-5793(98)00153-7;
RA   Kucharczyk R., Zagulski M., Rytka J., Herbert C.J.;
RT   "The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and
RT   is involved in nicotinic acid biosynthesis.";
RL   FEBS Lett. 424:127-130(1998).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-175 IN COMPLEX WITH DIVALENT
RP   METAL IONS, AND SUBUNIT.
RX   PubMed=16522801; DOI=10.1110/ps.051967906;
RA   Li X., Guo M., Fan J., Tang W., Wang D., Ge H., Rong H., Teng M., Niu L.,
RA   Liu Q., Hao Q.;
RT   "Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from
RT   Saccharomyces cerevisiae: a special subgroup of the type III extradiol
RT   dioxygenases.";
RL   Protein Sci. 15:761-773(2006).
CC   -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate
CC       to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes
CC       to quinolinate.
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         ECO:0000269|PubMed:9539135};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_03019,
CC       ECO:0000269|PubMed:9539135}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16522801}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03019,
CC       ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2330 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC       Rule:MF_03019}.
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DR   EMBL; Z49525; CAA89550.1; -; Genomic_DNA.
DR   EMBL; X87297; CAA60720.1; -; Genomic_DNA.
DR   EMBL; AY558309; AAS56635.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08814.1; -; Genomic_DNA.
DR   PIR; S57043; S57043.
DR   RefSeq; NP_012559.1; NM_001181683.1.
DR   PDB; 1ZVF; X-ray; 2.41 A; A/B=1-175.
DR   AlphaFoldDB; P47096; -.
DR   SMR; P47096; -.
DR   BioGRID; 33778; 130.
DR   DIP; DIP-4759N; -.
DR   FunCoup; P47096; 221.
DR   IntAct; P47096; 6.
DR   MINT; P47096; -.
DR   STRING; 4932.YJR025C; -.
DR   GlyGen; P47096; 1 site.
DR   iPTMnet; P47096; -.
DR   PaxDb; 4932-YJR025C; -.
DR   PeptideAtlas; P47096; -.
DR   EnsemblFungi; YJR025C_mRNA; YJR025C; YJR025C.
DR   GeneID; 853482; -.
DR   KEGG; sce:YJR025C; -.
DR   AGR; SGD:S000003786; -.
DR   SGD; S000003786; BNA1.
DR   VEuPathDB; FungiDB:YJR025C; -.
DR   eggNOG; KOG3995; Eukaryota.
DR   HOGENOM; CLU_095765_0_0_1; -.
DR   InParanoid; P47096; -.
DR   OMA; KPPVGNQ; -.
DR   OrthoDB; 204928at2759; -.
DR   BioCyc; MetaCyc:YJR025C-MONOMER; -.
DR   BioCyc; YEAST:YJR025C-MONOMER; -.
DR   BRENDA; 1.13.11.6; 984.
DR   Reactome; R-SCE-71240; Tryptophan catabolism.
DR   UniPathway; UPA00253; UER00330.
DR   BioGRID-ORCS; 853482; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P47096; -.
DR   PRO; PR:P47096; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47096; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IMP:SGD.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034354; P:'de novo' NAD+ biosynthetic process from L-tryptophan; IGI:SGD.
DR   GO; GO:0006569; P:L-tryptophan catabolic 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   CDD; cd06123; cupin_HAO; 1.
DR   FunFam; 2.60.120.10:FF:000093; 3-hydroxyanthranilate 3,4-dioxygenase; 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.
DR   PDBsum; 1ZVF; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..177
FT                   /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT                   /id="PRO_0000064375"
FT   BINDING         45
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         49
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT   BINDING         55
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         126
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   BINDING         129
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   BINDING         163
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   BINDING         166
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   HELIX           9..16
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   HELIX           17..20
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          77..83
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          87..91
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          106..112
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          121..125
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   HELIX           145..155
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:1ZVF"
FT   TURN            164..166
FT                   /evidence="ECO:0007829|PDB:1ZVF"
SQ   SEQUENCE   177 AA;  20235 MW;  930D69F486632417 CRC64;
     MFNTTPINID KWLKENEGLL KPPVNNYCLH KGGFTVMIVG GPNERTGYHI NPTPEWFYQK
     KGSMLLKVVD ETDAEPKFID IIINEGDSYL LPGNVPHSPV RFADTVGIVV EQDRPGGEND
     KIRWYCSHCR QVVHESELQM LDLGTQVKEA ILDFENDVEK RTCFHCKTLN YARPQSN
//