EQX3_GIBF5
ID EQX3_GIBF5 Reviewed; 373 AA.
AC S0DV66;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Diels-Alderase {ECO:0000303|PubMed:28379186};
DE Short=DA {ECO:0000303|PubMed:28379186};
DE EC=5.5.1.- {ECO:0000305|PubMed:28379186};
DE AltName: Full=Trichosetin biosynthesis cluster protein DA {ECO:0000303|PubMed:28379186};
GN Name=DA {ECO:0000303|PubMed:28379186}; ORFNames=FFUJ_02220;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=28379186; DOI=10.3390/toxins9040126;
RA Janevska S., Arndt B., Baumann L., Apken L.H., Mauriz Marques L.M.,
RA Humpf H.U., Tudzynski B.;
RT "Establishment of the inducible Tet-On system for the activation of the
RT silent trichosetin gene cluster in Fusarium fujikuroi.";
RL Toxins 9:0-0(2017).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of trichosetin, a trans-fused decalin-
CC containing tetramic acid with antimicrobial activity (PubMed:28379186).
CC The PKS module of PKS-NRPS1 together with the enoylreductase (ER)
CC catalyze the formation of the polyketide unit which is then conjugated
CC to L-serine by the condensation domain of the PKS-NRPS1 NRPS module (By
CC similarity). Activity of the Dieckmann cyclase domain (RED) results in
CC release of the Dieckmann product intermediate (By similarity). Diels-
CC Alderase (DA) is involved in endo-selective Diels-Alder cycloaddition
CC to form the decalin ring, leading to the production of N-
CC desmethylequisetin also called trichosetin (By similarity). The cluster
CC does not contain the equisetin N-methyltransferase and consequently,
CC trichosetin is isolated as final product (PubMed:28379186).
CC {ECO:0000250|UniProtKB:A0A0E4AZP0, ECO:0000269|PubMed:28379186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-3-[(2E,6R,8E,10E,12E)-2,6-dimethyltetradeca-2,8,10,12-
CC tetraenoyl]-5-(hydroxymethyl)pyrrolidine-2,4-dione = trichosetin;
CC Xref=Rhea:RHEA:67328, ChEBI:CHEBI:142061, ChEBI:CHEBI:169938;
CC Evidence={ECO:0000250|UniProtKB:A0A0E4AZP0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67329;
CC Evidence={ECO:0000250|UniProtKB:A0A0E4AZP0};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:28379186}.
CC -!- INDUCTION: Expression is positively regulated by the trichosetin
CC cluster-specific transcription activator TF22 (PubMed:28379186).
CC {ECO:0000269|PubMed:28379186}.
CC -!- DISRUPTION PHENOTYPE: Results in the production of reduced, though
CC significant, amounts of trichosetin (PubMed:28379186).
CC {ECO:0000269|PubMed:28379186}.
CC -!- SIMILARITY: Belongs to the Diels-Alderase family. {ECO:0000305}.
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DR EMBL; HF679025; CCT65287.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DV66; -.
DR SMR; S0DV66; -.
DR EnsemblFungi; CCT65287; CCT65287; FFUJ_02220.
DR VEuPathDB; FungiDB:FFUJ_02220; -.
DR HOGENOM; CLU_041924_2_0_1; -.
DR Proteomes; UP000016800; Chromosome 3.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Isomerase; Reference proteome.
FT CHAIN 1..373
FT /note="Diels-Alderase"
FT /id="PRO_0000443988"
SQ SEQUENCE 373 AA; 40673 MW; 7E58D4D43A0FBEEA CRC64;
MPAKTVSHLN FETSISTETV PASPYIPGSG NVFAKFVDAI SQTGWELWYF DGVSKDDQSA
ISIGINRSAR GLEHGGFTVQ IFAIWPDGHT WHRDLYFPES TVTSEDGHIT GLWEDAGSGG
KVSFSVTRDC SLTMLTFAVP GVVDGTMHLE TLPGDSGLET NPELGPRAHI VRPKGRASVK
AELSLSSGDN SASERFVLGP SANGGMDRIW TLDTWPKVMT ESYYLRAQVG PYAMQITRLF
SEAESGCKPY TMARLYRDGK LICAANQVLT YEEQDFSKDS LILSKRYDAS SEDVVTGAYR
DKNIGYVVEF VAKGTDGQRW MFQVDHERIF WSYPTSAPGP EGTGNTGFIE SVIGGADEEA
YFGVGIGGQC QLS