3HAO_HUMAN
ID 3HAO_HUMAN Reviewed; 286 AA.
AC P46952; A6NE56; B4DIN2; Q53QZ7; Q8N6N9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 187.
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, ECO:0000269|PubMed:7514594};
DE AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000255|HAMAP-Rule:MF_03019};
DE Short=3-HAO {ECO:0000255|HAMAP-Rule:MF_03019};
DE Short=h3HAO {ECO:0000303|PubMed:28375145};
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 {ECO:0000255|HAMAP-Rule:MF_03019, ECO:0000312|HGNC:HGNC:4796};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, COFACTOR, AND VARIANT VAL-37.
RX PubMed=7514594; DOI=10.1016/s0021-9258(17)36717-0;
RA Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R.,
RA Lahm H., Cesura A.M.;
RT "Molecular cloning and functional expression of human 3-hydroxyanthranilic-
RT acid dioxygenase.";
RL J. Biol. Chem. 269:13792-13797(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-37.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-37.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP INVOLVEMENT IN VCRL1, FUNCTION, PATHWAY, CATALYTIC ACTIVITY, VARIANTS VCRL1
RP 162-ASP--GLY-286 DEL AND 186-TRP--GLY-286 DEL, AND CHARACTERIZATION OF
RP VARIANTS VCRL1 162-ASP--GLY-286 DEL AND 186-TRP--GLY-286 DEL.
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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NICKEL IONS.
RG Center for eukaryotic structural genomics (CESG);
RT "Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [11] {ECO:0007744|PDB:5TK5, ECO:0007744|PDB:5TKQ}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT, AND
RP COFACTOR.
RX PubMed=28375145; DOI=10.1107/s2059798317002029;
RA Pidugu L.S., Neu H., Wong T.L., Pozharski E., Molloy J.L., Michel S.L.,
RA Toth E.A.;
RT "Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with
RT native and non-native metals bound in the active site.";
RL Acta Crystallogr. D 73:340-348(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 ECO:0000269|PubMed:28792876, ECO:0000269|PubMed:7514594}.
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:28792876, ECO:0000269|PubMed:7514594};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03019,
CC ECO:0000269|PubMed:28375145, ECO:0000269|PubMed:7514594};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_03019,
CC ECO:0000269|PubMed:28792876}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03019,
CC ECO:0000269|PubMed:28375145, ECO:0000269|Ref.10}.
CC -!- INTERACTION:
CC P46952; Q8IVA8: GAD1; NbExp=3; IntAct=EBI-743215, EBI-10209663;
CC P46952; Q99259: GAD1; NbExp=8; IntAct=EBI-743215, EBI-743184;
CC P46952; Q9NUX5: POT1; NbExp=2; IntAct=EBI-743215, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:7514594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P46952-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46952-2; Sequence=VSP_036239;
CC -!- DISEASE: Vertebral, cardiac, renal, and limb defects syndrome 1 (VCRL1)
CC [MIM:617660]: An autosomal recessive congenital malformation syndrome
CC characterized by vertebral segmentation abnormalities, congenital
CC cardiac defects, renal defects, and distal mild limb defects.
CC {ECO:0000269|PubMed:28792876}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
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DR EMBL; Z29481; CAA82618.1; -; mRNA.
DR EMBL; CR457063; CAG33344.1; -; mRNA.
DR EMBL; CR624693; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK295693; BAG58544.1; -; mRNA.
DR EMBL; AC098824; AAY14701.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00309.1; -; Genomic_DNA.
DR EMBL; BC029510; AAH29510.1; -; mRNA.
DR CCDS; CCDS33187.1; -. [P46952-1]
DR PIR; A54070; A54070.
DR RefSeq; NP_036337.2; NM_012205.2. [P46952-1]
DR PDB; 2QNK; X-ray; 1.60 A; A=2-286.
DR PDB; 5TK5; X-ray; 1.88 A; A=1-286.
DR PDB; 5TKQ; X-ray; 1.75 A; A=1-286.
DR PDBsum; 2QNK; -.
DR PDBsum; 5TK5; -.
DR PDBsum; 5TKQ; -.
DR AlphaFoldDB; P46952; -.
DR SMR; P46952; -.
DR BioGRID; 117047; 6.
DR IntAct; P46952; 5.
DR MINT; P46952; -.
DR STRING; 9606.ENSP00000294973; -.
DR BindingDB; P46952; -.
DR ChEMBL; CHEMBL3108657; -.
DR iPTMnet; P46952; -.
DR PhosphoSitePlus; P46952; -.
DR BioMuta; HAAO; -.
DR DMDM; 308153402; -.
DR EPD; P46952; -.
DR jPOST; P46952; -.
DR MassIVE; P46952; -.
DR MaxQB; P46952; -.
DR PaxDb; P46952; -.
DR PeptideAtlas; P46952; -.
DR PRIDE; P46952; -.
DR ProteomicsDB; 55777; -. [P46952-1]
DR ProteomicsDB; 55778; -. [P46952-2]
DR Antibodypedia; 29790; 183 antibodies from 32 providers.
DR DNASU; 23498; -.
DR Ensembl; ENST00000294973.11; ENSP00000294973.6; ENSG00000162882.15. [P46952-1]
DR GeneID; 23498; -.
DR KEGG; hsa:23498; -.
DR MANE-Select; ENST00000294973.11; ENSP00000294973.6; NM_012205.3; NP_036337.2.
DR UCSC; uc002rst.5; human. [P46952-1]
DR CTD; 23498; -.
DR DisGeNET; 23498; -.
DR GeneCards; HAAO; -.
DR HGNC; HGNC:4796; HAAO.
DR HPA; ENSG00000162882; Tissue enriched (liver).
DR MalaCards; HAAO; -.
DR MIM; 604521; gene.
DR MIM; 617660; phenotype.
DR neXtProt; NX_P46952; -.
DR OpenTargets; ENSG00000162882; -.
DR Orphanet; 521438; Congenital vertebral-cardiac-renal anomalies syndrome.
DR PharmGKB; PA29171; -.
DR VEuPathDB; HostDB:ENSG00000162882; -.
DR eggNOG; KOG3995; Eukaryota.
DR GeneTree; ENSGT00390000013008; -.
DR HOGENOM; CLU_064845_1_0_1; -.
DR InParanoid; P46952; -.
DR OMA; WQMEGSS; -.
DR OrthoDB; 1325876at2759; -.
DR PhylomeDB; P46952; -.
DR TreeFam; TF300246; -.
DR BioCyc; MetaCyc:HS08749-MON; -.
DR BRENDA; 1.13.11.6; 2681.
DR PathwayCommons; P46952; -.
DR Reactome; R-HSA-71240; Tryptophan catabolism.
DR SignaLink; P46952; -.
DR UniPathway; UPA00253; UER00330.
DR BioGRID-ORCS; 23498; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; HAAO; human.
DR EvolutionaryTrace; P46952; -.
DR GenomeRNAi; 23498; -.
DR Pharos; P46952; Tbio.
DR PRO; PR:P46952; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P46952; protein.
DR Bgee; ENSG00000162882; Expressed in right lobe of liver and 103 other tissues.
DR ExpressionAtlas; P46952; baseline and differential.
DR Genevisible; P46952; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046874; P:quinolinate metabolic process; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IDA:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Cytoplasm; Dioxygenase;
KW Disease variant; Iron; Metal-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..286
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000064372"
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 ECO:0000269|PubMed:28375145, ECO:0007744|PDB:5TK5"
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 ECO:0000269|PubMed:28375145, ECO:0007744|PDB:5TK5"
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 ECO:0000269|PubMed:28375145, ECO:0007744|PDB:5TK5"
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"
FT VAR_SEQ 148..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_036239"
FT VARIANT 37
FT /note="I -> V (in dbSNP:rs3816183)"
FT /evidence="ECO:0000269|PubMed:7514594, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.6"
FT /id="VAR_021507"
FT VARIANT 42
FT /note="T -> S (in dbSNP:rs3816182)"
FT /id="VAR_030470"
FT VARIANT 162..286
FT /note="Missing (in VCRL1; strongly reduced 3-
FT hydroxyanthranilate 3,4-dioxygenase activity in vitro)"
FT /evidence="ECO:0000269|PubMed:28792876"
FT /id="VAR_080252"
FT VARIANT 186..286
FT /note="Missing (in VCRL1; strongly reduced 3-
FT hydroxyanthranilate 3,4-dioxygenase activity in vitro)"
FT /evidence="ECO:0000269|PubMed:28792876"
FT /id="VAR_080253"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2QNK"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 24..37
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:2QNK"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:2QNK"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2QNK"
SQ SEQUENCE 286 AA; 32556 MW; 4DA6AC20FC6EC885 CRC64;
MERRLGVRAW VKENRGSFQP PVCNKLMHQE QLKVMFIGGP NTRKDYHIEE GEEVFYQLEG
DMVLRVLEQG KHRDVVIRQG EIFLLPARVP HSPQRFANTV GLVVERRRLE TELDGLRYYV
GDTMDVLFEK WFYCKDLGTQ LAPIIQEFFS SEQYRTGKPI PDQLLKEPPF PLSTRSIMEP
MSLDAWLDSH HRELQAGTPL SLFGDTYETQ VIAYGQGSSE GLRQNVDVWL WQLEGSSVVT
MGGRRLSLAP DDSLLVLAGT SYAWERTQGS VALSVTQDPA CKKPLG
