TOXD_DOTSN
ID TOXD_DOTSN Reviewed; 361 AA.
AC M2WKH6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Hps1-dma1 cluster oxidoreductase toxD {ECO:0000303|PubMed:31053329};
DE EC=1.-.-.- {ECO:0000305|PubMed:31053329};
GN Name=toxD; ORFNames=DOTSEDRAFT_28624;
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=31053329; DOI=10.1016/j.funbio.2019.02.006;
RA Ozturk I.K., Dupont P.Y., Chettri P., McDougal R., Boehl O.J., Cox R.J.,
RA Bradshaw R.E.;
RT "Evolutionary relics dominate the small number of secondary metabolism
RT genes in the hemibiotrophic fungus Dothistroma septosporum.";
RL Fungal Biol. 123:397-407(2019).
CC -!- FUNCTION: Oxidoreductase; part of the hps1-dma1 gene cluster that
CC probably mediates the biosynthesis a derivative of cyclopiazonic acid
CC (CPA) (Probable). The hybrid polyketide synthase-nonribosomal peptide
CC synthetase (PKS-NRPS) nps1 might incorporates acetyl-CoA, malonyl-CoA,
CC and tryptophan (Trp) and utilizes a C-terminal redox-incompetent
CC reductase domain to make and release the tryptophan tetramic acid,
CC cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in
CC the pathway (By similarity). In addition, the cluster also includes the
CC tryptophan dimethylallyltransferase dma1, the FAD-dependent
CC oxidoreductase toxD, the cytochrome P450 monooxygenase cyp3.1 and the
CC methyltransferase DOTSEDRAFT_139328; the latter 2 being not present in
CC all CPA-producing fungi but involved in additional modifications that
CC occur in biosynthesis of a range of CPA and CPA-like products
CC (Probable). Further studies are required to clarify whether the CPA-
CC like hps1-dma1 cluster is functional or a non-functional relic
CC reflecting evolution of D.septosporum (Probable).
CC {ECO:0000250|UniProtKB:B6F209, ECO:0000305|PubMed:31053329}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:31053329}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; KB446545; EME39478.1; -; Genomic_DNA.
DR AlphaFoldDB; M2WKH6; -.
DR SMR; M2WKH6; -.
DR STRING; 675120.M2WKH6; -.
DR EnsemblFungi; EME39478; EME39478; DOTSEDRAFT_28624.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_1_1; -.
DR OMA; YRMGTNE; -.
DR OrthoDB; 913304at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..361
FT /note="Hps1-dma1 cluster oxidoreductase toxD"
FT /id="PRO_0000447729"
FT BINDING 39..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 124..131
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 157..160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 180..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 260..261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 280..284
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 348..349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 361 AA; 38571 MW; D9B21F25AC0584AC CRC64;
MKAIKVNAGR TAAVQPARMP KLRDGYLLCK VHCVALNPAD WKYLDFIGVQ GVTLGADLSG
VVEEIDPSCG AHFEKGDRIA AFVHGGNVSQ PDDGAFAEYC LVKADLALKV PDAMSDEDAA
TLGVAVATCG QALYQGLELP LPGGAPYDGF LLVYGGSTST GTLAIQYARL SGCKVIATAS
PHNWPLLKEL GVEETFDYKD PDCAKKVRGI PICKAGYLTD GALIRAFTSD SLVLALDCIA
EGDSAKICED SISESKGGTI CYLFQAKHSR ADIVDKRVFA YTVFGEAFDK FGQSWPARAE
DFARGKEFAA LASQMLSDGQ LRPHPVRLGK DGLEGVLDGL QQLRERKVSG AKLVYRVVET
P
