ID   A0A1D9PW33_SCLS1        Unreviewed;       180 AA.
AC   A0A1D9PW33;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            EC=1.13.11.6 {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            Short=3-HAO {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            Short=HAD {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 1 {ECO:0000256|HAMAP-Rule:MF_03019};
GN   Name=BNA1 {ECO:0000256|HAMAP-Rule:MF_03019};
GN   ORFNames=sscle_02g016700 {ECO:0000313|EMBL:APA06900.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:APA06900.1, ECO:0000313|Proteomes:UP000177798};
RN   [1] {ECO:0000313|Proteomes:UP000177798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000177798};
RX   PubMed=28204478; DOI=10.1093/gbe/evx030;
RA   Derbyshire M., Denton-Giles M., Hegedus D., Seifbarghy S., Rollins J.,
RA   van Kan J., Seidl M.F., Faino L., Mbengue M., Navaud O., Raffaele S.,
RA   Hammond-Kosack K., Heard S., Oliver R.;
RT   "The complete genome sequence of the phytopathogenic fungus Sclerotinia
RT   sclerotiorum reveals insights into the genome architecture of broad host
RT   range pathogens.";
RL   Genome Biol. Evol. 9:593-618(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:0000256|ARBA:ARBA00002752, ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-Rule:MF_03019};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|HAMAP-Rule:MF_03019};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 3/3. {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000256|HAMAP-
CC       Rule:MF_03019}.
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DR   EMBL; CP017815; APA06900.1; -; Genomic_DNA.
DR   RefSeq; XP_001594643.1; XM_001594593.1.
DR   AlphaFoldDB; A0A1D9PW33; -.
DR   EnsemblFungi; EDO01975; EDO01975; SS1G_04451.
DR   GeneID; 5490816; -.
DR   KEGG; ssl:SS1G_04451; -.
DR   VEuPathDB; FungiDB:sscle_02g016700; -.
DR   OMA; KPPVGNQ; -.
DR   OrthoDB; 2907058at2759; -.
DR   UniPathway; UPA00253; UER00330.
DR   Proteomes; UP000177798; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
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: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 {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_03019}.
FT   REGION          160..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         48
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         92
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         121
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         124
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         158
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
SQ   SEQUENCE   180 AA;  20397 MW;  8E2B82606D209D02 CRC64;
     MLTAPLNLPK WLEENSHLLK PPINNYCVYN KDVTVMIVGG PNARTDYHIN ETAEWFYQYK
     GAMMLKVVDE GEFKDIIIGE GEMFLLPPNT PHNPVRFANT VGIVLEQPRP KDSLDRLRWY
     CTNCREVVEE AAFHCTDLGT QIKEAVNSFK DSEERRKCKK CGTVAESAPP PGSIQDPNLS
//

ID   A7EGK9_SCLS1            Unreviewed;       180 AA.
AC   A7EGK9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            EC=1.13.11.6 {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            Short=3-HAO {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            Short=HAD {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 1 {ECO:0000256|HAMAP-Rule:MF_03019};
GN   Name=BNA1 {ECO:0000256|HAMAP-Rule:MF_03019};
GN   ORFNames=SS1G_04451 {ECO:0000313|EMBL:EDO01975.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO01975.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate
CC       to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes
CC       to quinolinate. {ECO:0000256|ARBA:ARBA00002752, ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-Rule:MF_03019};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|HAMAP-Rule:MF_03019};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 3/3. {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000256|HAMAP-
CC       Rule:MF_03019}.
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DR   EMBL; CH476625; EDO01975.1; -; Genomic_DNA.
DR   RefSeq; XP_001594643.1; XM_001594593.1.
DR   AlphaFoldDB; A7EGK9; -.
DR   STRING; 665079.A7EGK9; -.
DR   EnsemblFungi; EDO01975; EDO01975; SS1G_04451.
DR   GeneID; 5490816; -.
DR   KEGG; ssl:SS1G_04451; -.
DR   VEuPathDB; FungiDB:sscle_02g016700; -.
DR   eggNOG; KOG3995; Eukaryota.
DR   HOGENOM; CLU_095765_0_0_1; -.
DR   InParanoid; A7EGK9; -.
DR   OMA; KPPVGNQ; -.
DR   OrthoDB; 2907058at2759; -.
DR   UniPathway; UPA00253; UER00330.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
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; 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 {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_03019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT   REGION          160..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         48
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         92
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         121
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         124
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         158
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
SQ   SEQUENCE   180 AA;  20397 MW;  8E2B82606D209D02 CRC64;
     MLTAPLNLPK WLEENSHLLK PPINNYCVYN KDVTVMIVGG PNARTDYHIN ETAEWFYQYK
     GAMMLKVVDE GEFKDIIIGE GEMFLLPPNT PHNPVRFANT VGIVLEQPRP KDSLDRLRWY
     CTNCREVVEE AAFHCTDLGT QIKEAVNSFK DSEERRKCKK CGTVAESAPP PGSIQDPNLS
//