ID R4XH29_TAPDE Unreviewed; 470 AA.
AC R4XH29;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 13-SEP-2023, entry version 35.
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=TAPDE_005572 {ECO:0000313|EMBL:CCG84998.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG84998.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG84998.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03019}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCG84998.1}.
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DR EMBL; CAHR02000378; CCG84998.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XH29; -.
DR STRING; 1097556.R4XH29; -.
DR VEuPathDB; FungiDB:TAPDE_005572; -.
DR eggNOG; KOG2644; Eukaryota.
DR eggNOG; KOG3995; Eukaryota.
DR UniPathway; UPA00253; UER00330.
DR Proteomes; UP000013776; Unassembled WGS sequence.
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; cd00885; cinA; 1.
DR CDD; cd06123; cupin_HAO; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR HAMAP; MF_00825; 3_HAO; 1.
DR InterPro; IPR010329; 3hydroanth_dOase.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR NCBIfam; TIGR03037; anthran_nbaC; 1.
DR PANTHER; PTHR47675; MOLYBDOPTERIN BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_5G11210); 1.
DR PANTHER; PTHR47675:SF1; MOLYBDOPTERIN BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_5G11210); 1.
DR Pfam; PF06052; 3-HAO; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 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:UP000013776}.
FT DOMAIN 8..179
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT BINDING 340
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT BINDING 344
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT BINDING 389
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03019"
SQ SEQUENCE 470 AA; 52592 MW; A47B2C2164EA6CEA CRC64;
MQQIRTAGIV IIGDEVLSSK TVDTNSAWFA KYCFELGIDL KRIEIIADDE SEIVEAVTRM
SSKYDFVVTS GGIGPTHDDI TYPSIAKAFN NKLTYHDETL ERMKKLSVRP INWDVPADDP
ELVARKRMAL FPTPSQIVYP SEKLWVPIVI AGGNVHILPG IPRLFTGLLS EYRKTIVDNV
DPAMKQTRIL ISTGLPESAI SKYLGDLQKK VDAKGVKVGS YPKGIGMGVM ISLLGRDLSY
LETLVADVEK SLDGKRVDVE AEAQNEVDRT KAEKERMNSS ENYKLDLPAI PENLGPISPP
INFPLWLKEN GHLLQPPVNN FCLYAEKDFI VMTVGGPNAR NDYHINNTEE WFYQYKGDML
LKVVEGGTTF KDIPIKEGEM FLLPANTPHN PVRFANTIGI VIERVRPDTS RDKLRWYCSS
GNHSKPTIVA ETNLGHVTNL GTQLKPAIQQ WQEDETMRTC KECGEIMPAK
//