3HAO_XENTR
ID 3HAO_XENTR Reviewed; 280 AA.
AC Q6DIZ0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
CC -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000255|HAMAP-
CC Rule:MF_03019}.
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DR EMBL; BC075395; AAH75395.1; -; mRNA.
DR RefSeq; NP_001006914.1; NM_001006913.1.
DR RefSeq; XP_017949333.1; XM_018093844.1.
DR AlphaFoldDB; Q6DIZ0; -.
DR SMR; Q6DIZ0; -.
DR STRING; 8364.ENSXETP00000061535; -.
DR PaxDb; Q6DIZ0; -.
DR DNASU; 448761; -.
DR GeneID; 448761; -.
DR KEGG; xtr:448761; -.
DR CTD; 23498; -.
DR Xenbase; XB-GENE-5800903; haao.
DR eggNOG; KOG3995; Eukaryota.
DR InParanoid; Q6DIZ0; -.
DR OrthoDB; 1325876at2759; -.
DR Reactome; R-XTR-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00330.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0019805; P:quinolinate biosynthetic process; ISS:UniProtKB.
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; 2.
DR TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..280
FT /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT /id="PRO_0000245468"
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..280
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 280 AA; 32335 MW; 4E679AB7C625FA97 CRC64;
MAIPVNVKKW IDENREYFLP PVCNKLMQNH QLKVMFVGGP NQRKDYHIEE GEELFYQVQG
DMCLKIVENG KHKDVHIKEG EMFLLPGRIP HSPQRYADTV GLVFERRRLD TEKDGLRYYV
EGTTEVLFEK WFYCEDLGTQ LAPIMKEFFS SEQYKSGKPD PAQPIGKMPF FLNTEQVMEP
FSFQNWLNKH RLEINQKKRV SLFGHNQETK AVVYGSGESK DSKAQTDTWI WQLEGTSCVT
LGNEVLKLGS GDSLLIPEKS LYSWIREDCS IALSTSQVPA
