DMA1_DOTSN
ID DMA1_DOTSN Reviewed; 420 AA.
AC M2Y2F4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Tryptophan dimethylallyltransferase dma1 {ECO:0000303|PubMed:31053329};
DE EC=2.5.1.- {ECO:0000305|PubMed:31053329};
DE AltName: Full=L-tryptophan dimethylallyl transferase {ECO:0000305};
DE Short=DMATS {ECO:0000305};
GN Name=dma1 {ECO:0000303|PubMed:31053329}; ORFNames=DOTSEDRAFT_28625;
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, INDUCTION, DOMAIN, 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: Tryptophan dimethylallyltransferase; part of the hps1-dma1
CC gene cluster that probably mediates the biosynthesis a derivative of
CC cyclopiazonic acid (CPA) (Probable). The hybrid polyketide synthase-
CC nonribosomal peptide synthetase (PKS-NRPS) nps1 might incorporates
CC acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal
CC redox-incompetent reductase domain to make and release the tryptophan
CC tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first
CC intermediate in the pathway (By similarity). In addition, the cluster
CC also includes the tryptophan dimethylallyltransferase dma1, the FAD-
CC dependent oxidoreductase toxD, the cytochrome P450 monooxygenase cyp3.1
CC and the methyltransferase DOTSEDRAFT_139328; the latter 2 being not
CC present in all CPA-producing fungi but involved in additional
CC modifications that occur in biosynthesis the of a range of CPA and CPA-
CC like products (Probable). Further studies are required to clarify
CC whether the CPA-like hps1-dma1 cluster is functional or a non-
CC functional relic 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 -!- INDUCTION: Barely expressed under any of the conditions tested.
CC {ECO:0000269|PubMed:31053329}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KB446545; EME39479.1; -; Genomic_DNA.
DR AlphaFoldDB; M2Y2F4; -.
DR SMR; M2Y2F4; -.
DR STRING; 675120.M2Y2F4; -.
DR EnsemblFungi; EME39479; EME39479; DOTSEDRAFT_28625.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_4_0_1; -.
DR OMA; HNEPEPY; -.
DR OrthoDB; 1465213at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..420
FT /note="Tryptophan dimethylallyltransferase dma1"
FT /id="PRO_0000447727"
FT BINDING 65..66
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 420 AA; 47348 MW; 42F794817C81E31D CRC64;
MVEIQSQNEH HKFWANHLLP QFRRYIAEIG AYTSKQQDEH VKFFDSLLPH LGPRLPHPHT
KAVLTVANMP LGFSVNLSDA RKPIARMEIE PLDDTSGSAE DLFAANCIPA CFTTLVKGMT
TRVDTRWAHQ LRQAFTPTSE ESAIAKPRLR PGIERVSLAY FGITFDGDNR AMKYCTSHWP
KFLGTATAES NDATSADAFL FSAIRRLKPG GEALAPSLDA IQHYFQNERH AKLPSPILFV
GLDCIDPSRA RIKMYGRTHS TAFSNVRNIM TLGGRALTAE TTEFLARLRS IWHLLLNDPK
AKDDEDYDRP PLDPNSLRTG LLVSFEVSAL VSTPDIKVYV PFWQYHETDV QAINNLEQIF
SLLGWDWGSG KYGDLLRKTF VGTDLAATQN HDYVSFNYSK RQGSYMTMYH VPPRPESTTA
