3HAO_MOUSE
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 03-AUG-2022, entry version 148.
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;
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 -!- 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; Q78JT3; -.
DR PeptideAtlas; Q78JT3; -.
DR PRIDE; Q78JT3; -.
DR ProteomicsDB; 285816; -.
DR Antibodypedia; 29790; 183 antibodies from 32 providers.
DR DNASU; 107766; -.
DR Ensembl; ENSMUST00000000687; ENSMUSP00000000687; ENSMUSG00000000673.
DR GeneID; 107766; -.
DR KEGG; mmu:107766; -.
DR UCSC; uc008dsk.1; mouse.
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; WQMEGSS; -.
DR OrthoDB; 1325876at2759; -.
DR PhylomeDB; Q78JT3; -.
DR TreeFam; TF300246; -.
DR Reactome; R-MMU-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00330.
DR BioGRID-ORCS; 107766; 4 hits in 74 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 60 other tissues.
DR ExpressionAtlas; Q78JT3; baseline and differential.
DR Genevisible; Q78JT3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; -; 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 PANTHER; PTHR15497; PTHR15497; 1.
DR Pfam; PF06052; 3-HAO; 1.
DR PIRSF; PIRSF017681; 3hydroanth_dOase_animal; 1.
DR SUPFAM; SSF51182; SSF51182; 2.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
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
