3HAO_CAEEL
ID 3HAO_CAEEL Reviewed; 281 AA.
AC Q19341; Q21258;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 151.
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-1; ORFNames=K06A4.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03019}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
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DR EMBL; Z70755; CAA94787.1; -; Genomic_DNA.
DR EMBL; Z70751; CAA94787.1; JOINED; Genomic_DNA.
DR PIR; T20743; T20743.
DR RefSeq; NP_505450.1; NM_073049.1.
DR AlphaFoldDB; Q19341; -.
DR SMR; Q19341; -.
DR BioGRID; 44367; 5.
DR IntAct; Q19341; 5.
DR MINT; Q19341; -.
DR STRING; 6239.K06A4.5; -.
DR World-2DPAGE; 0011:Q19341; -.
DR EPD; Q19341; -.
DR PaxDb; Q19341; -.
DR PeptideAtlas; Q19341; -.
DR EnsemblMetazoa; K06A4.5.1; K06A4.5.1; WBGene00010595.
DR EnsemblMetazoa; K06A4.5.2; K06A4.5.2; WBGene00010595.
DR GeneID; 179329; -.
DR KEGG; cel:CELE_K06A4.5; -.
DR UCSC; K06A4.5; c. elegans.
DR CTD; 179329; -.
DR WormBase; K06A4.5; CE06109; WBGene00010595; haao-1.
DR eggNOG; KOG3995; Eukaryota.
DR GeneTree; ENSGT00390000013008; -.
DR HOGENOM; CLU_064845_0_0_1; -.
DR InParanoid; Q19341; -.
DR OMA; WQMEGSS; -.
DR OrthoDB; 1325876at2759; -.
DR PhylomeDB; Q19341; -.
DR Reactome; R-CEL-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00330.
DR PRO; PR:Q19341; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010595; Expressed in larva and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
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: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; 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; 1.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..281
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000245470"
FT REGION 1..162
FT /note="Domain A (catalytic)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT REGION 163..179
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT REGION 180..281
FT /note="Domain B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 55
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
SQ SEQUENCE 281 AA; 32227 MW; E3DD76D60D5930A9 CRC64;
MSGVTAIEIP QWIQDNQEDF VPPVCNKCMF SDQLKVFYVG GPNQRKDFHL EEGEEFFFQR
KGDMVLKVIE KGQVRDLVIK QGEMFMLPAR VEHSPQRFSN SIGLVVERER KNTEFDCVRF
LVGSSNITLF ERWFYLTDVV KDLPPLIKEF YGSNEFKTGK PGKGTFACNA PYEARWTDLP
VPINRKEFIY DHISEVKNGP VRIYGAPEYK TEVMLLGEGS YDLESGTVEL LIWLQENTFA
VVEESGFTYA MKSETMVRIK PNTKCLLNVK GGFAITIRMP A
