位置:首页 > 蛋白库 > DMA1_DOTSN
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024