ID   3HAO_DICDI              Reviewed;         182 AA.
AC   Q54S02;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
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; ORFNames=DDB_G0282743;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AAFI02000047; EAL66231.1; -; Genomic_DNA.
DR   RefSeq; XP_640237.1; XM_635145.1.
DR   AlphaFoldDB; Q54S02; -.
DR   SMR; Q54S02; -.
DR   STRING; 44689.Q54S02; -.
DR   PaxDb; 44689-DDB0231359; -.
DR   EnsemblProtists; EAL66231; EAL66231; DDB_G0282743.
DR   GeneID; 8623776; -.
DR   KEGG; ddi:DDB_G0282743; -.
DR   dictyBase; DDB_G0282743; haao.
DR   eggNOG; KOG3995; Eukaryota.
DR   HOGENOM; CLU_095765_0_0_1; -.
DR   InParanoid; Q54S02; -.
DR   OMA; KPPVGNQ; -.
DR   PhylomeDB; Q54S02; -.
DR   Reactome; R-DDI-71240; Tryptophan catabolism.
DR   UniPathway; UPA00253; UER00330.
DR   PRO; PR:Q54S02; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; ISS:dictyBase.
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:0009435; P:NAD biosynthetic process; ISS:dictyBase.
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; Jelly Rolls; 1.
DR   HAMAP; MF_00825; 3_HAO; 1.
DR   InterPro; IPR010329; 3hydroanth_dOase.
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   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..182
FT                   /note="3-hydroxyanthranilate 3,4-dioxygenase"
FT                   /id="PRO_0000328344"
FT   BINDING         46
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         95
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         124
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         129
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         165
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
FT   BINDING         168
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03019"
SQ   SEQUENCE   182 AA;  21210 MW;  AB372715BAA44ED4 CRC64;
     MLPPININKW IEENKSLLQP PVGAKLLYTD IDSTFVVMIV GGPNQRTDYH VNETDEFFYQ
     FKGDMILKIV DKDGSFRDIN IREGETFILP GNTPHSPQRY RDTIGLVIEK KRSSENIDKL
     LWFCDNKDCR KLLFSRSFHV DDLDLGKQLT PIINEFYGNE ENRTCKHCNH ISQKPTVNDY
     IQ
//