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   24-JAN-2024, entry version 195.
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,
GN   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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03019, ECO:0000269|PubMed:28375145,
CC         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 9606-ENSP00000294973; -.
DR   PeptideAtlas; P46952; -.
DR   ProteomicsDB; 55777; -. [P46952-1]
DR   ProteomicsDB; 55778; -. [P46952-2]
DR   Antibodypedia; 29790; 203 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   AGR; HGNC:4796; -.
DR   CTD; 23498; -.
DR   DisGeNET; 23498; -.
DR   GeneCards; HAAO; -.
DR   GeneReviews; 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; WQRNEGT; -.
DR   OrthoDB; 2907058at2759; -.
DR   PhylomeDB; P46952; -.
DR   TreeFam; TF300246; -.
DR   BioCyc; MetaCyc:HS08749-MONOMER; -.
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 1144 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 104 other cell types or tissues.
DR   ExpressionAtlas; P46952; baseline and differential.
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; 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; P46952; HS.
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
FT                   3-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
FT                   3-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
//