DMAT1_GIBF5
ID DMAT1_GIBF5 Reviewed; 419 AA.
AC S0EH60;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Dimethylallyltryptophan synthase 1 {ECO:0000303|PubMed:28295904};
DE Short=DMATS 1 {ECO:0000303|PubMed:28295904};
DE EC=2.5.1.- {ECO:0000269|PubMed:28295904};
DE AltName: Full=DMATS1 biosynthesis cluster protein DMATS1 {ECO:0000303|PubMed:28295904};
GN Name=DMATS1 {ECO:0000303|PubMed:28295904}; ORFNames=FFUJ_09179;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28295904; DOI=10.1002/cbic.201600691;
RA Arndt B., Janevska S., Schmid R., Huebner F., Tudzynski B., Humpf H.U.;
RT "A Fungal N-Dimethylallyltryptophan Metabolite from Fusarium fujikuroi.";
RL ChemBioChem 18:899-904(2017).
CC -!- FUNCTION: Dimethylallyltryptophan synthase; part of the DMATS1 gene
CC cluster that mediates the biosynthesis of a reversely N-prenylated
CC monomeric L-tryptophan (r-N-DMAT) (PubMed:28295904). The main product
CC of the cluster is the r-N-DMAT produced by the dimethylallyltryptophan
CC synthase DMATS1 and it remains unclear whether this metabolite
CC undergoes further modifications when silent gene clusters are activated
CC (PubMed:28295904). The acetylated form of r-N-DMAT, ac-r-N-DMAT, is
CC also produced (PubMed:28295904). The roles of the cytochrome P450
CC monooxygenase FFUJ_09176 and the methyltransferase FFUJ_09178 have
CC still to be elucidated (Probable). {ECO:0000269|PubMed:28295904,
CC ECO:0000305|PubMed:28295904}.
CC -!- INDUCTION: Expression is negaticely regulated by the global nitrogen
CC regulator areA. {ECO:0000269|PubMed:28295904}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of r-N-DMAT and ac-r-N-
CC DMAT. {ECO:0000269|PubMed:28295904}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HF679031; CCT73985.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EH60; -.
DR SMR; S0EH60; -.
DR EnsemblFungi; CCT73985; CCT73985; FFUJ_09179.
DR VEuPathDB; FungiDB:FFUJ_09179; -.
DR HOGENOM; CLU_037431_2_2_1; -.
DR Proteomes; UP000016800; Chromosome 9.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="Dimethylallyltryptophan synthase 1"
FT /id="PRO_0000452656"
FT BINDING 81..82
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 90
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 189
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 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 419 AA; 47291 MW; 3F82AC79D784095D CRC64;
MLLQASQATQ SVWKTLNKWL PPLSRDKDWW WKTLGPQINT LLTEADYDLN ERYEALLLLY
RWVVPEMGPR PRSSVAPSKS FMTDDHSPIE YSWKWISGNK KPEIRYAVEL VSPLAGSKQD
PFNQIPTRNL VYNLAKIIPE LDLTWFEHFW HELLGPGSPT TSTSGVLTKG STVFAALEML
HGHLSVKVYF IPVETPDFSA WHQIKHAIEA SGCPNLEALN HVDAYLSSHD DGRQLRPFML
AIDLVEPAAS RLKIYARSNQ TSFRFVRDVM TIGGLRTDLD RSIEKFSDLW KRALGLDPDT
PPEDELPKVD HLTSGAVFNF DVAPKSQIPE VKAYIPVRHY ANNDLQAALG LIGYLEDHGH
GGYSQSYLRG LDMLAPSGQL DQATGVQTYF AVACQGEDLS LTSYLNPQFY AAFQEPERT
