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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
 
 
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