EQXC_GIBF5
ID EQXC_GIBF5 Reviewed; 355 AA.
AC S0DXU0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Trans-enoyl reductase {ECO:0000303|PubMed:28379186};
DE Short=ER {ECO:0000303|PubMed:28379186};
DE EC=1.-.-.- {ECO:0000305|PubMed:28379186};
DE AltName: Full=Trichosetin biosynthesis cluster protein ER {ECO:0000303|PubMed:28379186};
GN Name=ER {ECO:0000303|PubMed:28379186}; ORFNames=FFUJ_02221;
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=acetyl-CoA + ATP + 11 H(+) + L-serine + 7 malonyl-CoA + 8
CC NADPH + 2 S-adenosyl-L-methionine = (5S)-3-[(2E,6R,8E,10E,12E)-2,6-
CC dimethyltetradeca-2,8,10,12-tetraenoyl]-5-(hydroxymethyl)pyrrolidine-
CC 2,4-dione + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + 8 NADP(+) + 2
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67324, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58349, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:169938, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:A0A0E4AZP0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67325;
CC Evidence={ECO:0000250|UniProtKB:A0A0E4AZP0};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:28379186}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
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: Completely abolishes trichosetin production
CC (PubMed:28379186). {ECO:0000269|PubMed:28379186}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; HF679025; CCT65288.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DXU0; -.
DR SMR; S0DXU0; -.
DR STRING; 1279085.S0DXU0; -.
DR EnsemblFungi; CCT65288; CCT65288; FFUJ_02221.
DR VEuPathDB; FungiDB:FFUJ_02221; -.
DR HOGENOM; CLU_026673_16_1_1; -.
DR Proteomes; UP000016800; Chromosome 3.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..355
FT /note="Trans-enoyl reductase"
FT /id="PRO_0000443989"
FT BINDING 45..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 131..138
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 166..169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 189..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 254..255
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 275..279
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 344..345
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 355 AA; 38456 MW; 0983706C7EF93750 CRC64;
MVQRLQSALV GTPEGGIRLS TTEIVPDITG DSVLVKTKAV SVNPVDTKMI GPYVTPGAVA
GFDFAGVVEQ VGPEATKCDI HVGDRVCTAI MGMNPLDPHV GAFSEYTAAV EWILLKIPPH
LSFEEGASLG ISFMTTGLAL FKSLGLPGNP IEPATEPMPV LVYGGSSATG TAAVQLVKLA
GFEPIATCSP RNFDLVKSYG ASAVFDYQDP NCTSDIRKHT KNKIKYALDC ISTTSSMQFC
YQAIGRAGGK YTALEPYSEA VARTRKVVKP DWIMGPQMLG KEIRWPEPHW RPANAEMGEF
GVYWTAVLRR LLDKGLIRPH HIVVKQGGLA EVLHGIEDIR EKRISGKKLV FQMEI
