3HAO_YEAST
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 03-AUG-2022, entry version 179.
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 PDBsum; 1ZVF; -.
DR AlphaFoldDB; P47096; -.
DR SMR; P47096; -.
DR BioGRID; 33778; 115.
DR DIP; DIP-4759N; -.
DR IntAct; P47096; 1.
DR MINT; P47096; -.
DR STRING; 4932.YJR025C; -.
DR iPTMnet; P47096; -.
DR MaxQB; P47096; -.
DR PaxDb; P47096; -.
DR PRIDE; P47096; -.
DR EnsemblFungi; YJR025C_mRNA; YJR025C; YJR025C.
DR GeneID; 853482; -.
DR KEGG; sce:YJR025C; -.
DR SGD; S000003786; BNA1.
DR VEuPathDB; FungiDB:YJR025C; -.
DR eggNOG; KOG3995; Eukaryota.
DR GeneTree; ENSGT00390000013008; -.
DR HOGENOM; CLU_095765_0_0_1; -.
DR InParanoid; P47096; -.
DR OMA; NARKDYH; -.
DR BioCyc; MetaCyc:YJR025C-MON; -.
DR BioCyc; YEAST:YJR025C-MON; -.
DR BRENDA; 1.13.11.6; 984.
DR Reactome; R-SCE-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00330.
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 tryptophan; IGI:SGD.
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; -; 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 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
