ID   3HAO_MOUSE              Reviewed;         286 AA.
AC   Q78JT3; Q52L88;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 156.
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};
GN   Name=Haao;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=28792876; DOI=10.1056/nejmoa1616361;
RA   Shi H., Enriquez A., Rapadas M., Martin E.M.M.A., Wang R., Moreau J.,
RA   Lim C.K., Szot J.O., Ip E., Hughes J.N., Sugimoto K., Humphreys D.T.,
RA   McInerney-Leo A.M., Leo P.J., Maghzal G.J., Halliday J., Smith J.,
RA   Colley A., Mark P.R., Collins F., Sillence D.O., Winlaw D.S., Ho J.W.K.,
RA   Guillemin G.J., Brown M.A., Kikuchi K., Thomas P.Q., Stocker R.,
RA   Giannoulatou E., Chapman G., Duncan E.L., Sparrow D.B., Dunwoodie S.L.;
RT   "NAD deficiency, congenital malformations, and niacin supplementation.";
RL   N. Engl. J. Med. 377:544-552(2017).
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   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03019,
CC       ECO:0000269|PubMed:28792876}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC       Rule:MF_03019}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice were born at the
CC       expected Mendelian ratio and are normal. They however show very high
CC       levels of 3-hydroxyanthranilate compared to wild-type mice.
CC       {ECO:0000269|PubMed:28792876}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC       Rule:MF_03019}.
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DR   EMBL; BC012872; AAH12872.1; -; mRNA.
DR   EMBL; BC094021; AAH94021.1; -; mRNA.
DR   CCDS; CCDS37709.1; -.
DR   RefSeq; NP_079601.1; NM_025325.2.
DR   RefSeq; XP_006523526.1; XM_006523463.3.
DR   AlphaFoldDB; Q78JT3; -.
DR   SMR; Q78JT3; -.
DR   IntAct; Q78JT3; 1.
DR   MINT; Q78JT3; -.
DR   STRING; 10090.ENSMUSP00000000687; -.
DR   iPTMnet; Q78JT3; -.
DR   PhosphoSitePlus; Q78JT3; -.
DR   EPD; Q78JT3; -.
DR   jPOST; Q78JT3; -.
DR   MaxQB; Q78JT3; -.
DR   PaxDb; 10090-ENSMUSP00000000687; -.
DR   PeptideAtlas; Q78JT3; -.
DR   ProteomicsDB; 285816; -.
DR   Antibodypedia; 29790; 203 antibodies from 32 providers.
DR   DNASU; 107766; -.
DR   Ensembl; ENSMUST00000000687.9; ENSMUSP00000000687.8; ENSMUSG00000000673.10.
DR   GeneID; 107766; -.
DR   KEGG; mmu:107766; -.
DR   UCSC; uc008dsk.1; mouse.
DR   AGR; MGI:1349444; -.
DR   CTD; 23498; -.
DR   MGI; MGI:1349444; Haao.
DR   VEuPathDB; HostDB:ENSMUSG00000000673; -.
DR   eggNOG; KOG3995; Eukaryota.
DR   GeneTree; ENSGT00390000013008; -.
DR   HOGENOM; CLU_064845_1_0_1; -.
DR   InParanoid; Q78JT3; -.
DR   OMA; WQRNEGT; -.
DR   OrthoDB; 2907058at2759; -.
DR   PhylomeDB; Q78JT3; -.
DR   TreeFam; TF300246; -.
DR   Reactome; R-MMU-71240; Tryptophan catabolism.
DR   UniPathway; UPA00253; UER00330.
DR   BioGRID-ORCS; 107766; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Haao; mouse.
DR   PRO; PR:Q78JT3; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q78JT3; Protein.
DR   Bgee; ENSMUSG00000000673; Expressed in right kidney and 62 other cell types or tissues.
DR   ExpressionAtlas; Q78JT3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IDA:MGI.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR   GO; GO:0019825; F:oxygen binding; ISO:MGI.
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:0009435; P:NAD biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0046874; P:quinolinate metabolic process; ISO:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; ISO:MGI.
DR   GO; GO:0010043; P:response to zinc ion; ISO:MGI.
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; IPR016700; 3hydroanth_dOase_met.
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   PIRSF; PIRSF017681; 3hydroanth_dOase_animal; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 2.
DR   Genevisible; Q78JT3; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..286
FT                   /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT                   /id="PRO_0000064373"
FT   REGION          1..160
FT                   /note="Domain A (catalytic)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   REGION          161..177
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   REGION          178..286
FT                   /note="Domain B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         43
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         47
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         53
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
SQ   SEQUENCE   286 AA;  32804 MW;  CD8A706EE264B4CD CRC64;
     MERRVRVKSW VEENRASFQP PVCNKLMHQE QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG
     DMILRVLEQG QHRDVPIRQG EIFLLPARVP HSPQRFANTM GLVIERRRLE SELDGLRYYV
     GDTEDVLFEK WFHCKDLGTQ LAPIIQEFFH SEQYRTGKPN PDQLLKELPF PLNTRSIMKP
     MSLKAWLDGH SRELQAGTSL SLFGDSYETQ VIAHGQGSSK GPRQDVDVWL WQQEGSSKVT
     MGGQCIALAP DDSLLVPAGT SYVWERAQGS VALSVTQDPA RKKPWW
//