ID   FUJ2_GIBF5              Reviewed;         346 AA.
AC   S0EJ18;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Trans-enoyl reductase FFUJ_12240 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   AltName: Full=Fujikurins biosynthesis cluster protein FFUJ_12240 {ECO:0000303|PubMed:26192387};
GN   ORFNames=FFUJ_12240;
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], IDENTIFICATION, FUNCTION,
RP   AND INDUCTION.
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.
RX   PubMed=26192387; DOI=10.1021/np5008137;
RA   von Bargen K.W., Niehaus E.M., Krug I., Bergander K., Wuerthwein E.U.,
RA   Tudzynski B., Humpf H.U.;
RT   "Isolation and structure elucidation of fujikurins A-D: products of the
RT   PKS19 gene cluster in Fusarium fujikuroi.";
RL   J. Nat. Prod. 78:1809-1815(2015).
CC   -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC       the biosynthesis of fujikurins A-D, secondary metabolites playing a
CC       role during rice infection (PubMed:23825955, PubMed:26192387). The
CC       polyketide synthase PKS19 acts with the trans-enoyl reductase
CC       FFUJ_12240 and the polyketide transferase FFUJ_12241 to produce
CC       fujikurins, however, the biosynthesis pathway has not been identified
CC       yet (PubMed:23825955, PubMed:26192387). {ECO:0000269|PubMed:23825955,
CC       ECO:0000269|PubMed:26192387}.
CC   -!- INDUCTION: The fujikurins gene cluster is specifically expressed during
CC       rice infection (PubMed:23825955). {ECO:0000269|PubMed:23825955}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; HF679030; CCT72378.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EJ18; -.
DR   SMR; S0EJ18; -.
DR   STRING; 1279085.S0EJ18; -.
DR   EnsemblFungi; CCT72378; CCT72378; FFUJ_12240.
DR   VEuPathDB; FungiDB:FFUJ_12240; -.
DR   HOGENOM; CLU_026673_16_1_1; -.
DR   Proteomes; UP000016800; Chromosome 8.
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..346
FT                   /note="Trans-enoyl reductase FFUJ_12240"
FT                   /id="PRO_0000442009"
FT   BINDING         40..43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         124..131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         157..160
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         180..183
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         245..246
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         266..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         335..336
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   346 AA;  36683 MW;  0D0E46D261E5FEB4 CRC64;
     MQALVGAETG GYRLADNVEK PVLQPGSILC HVKAVALNPH DAKIVDYSNV PGALGGCDFA
     GVVVEIGNGV KRFKEGDRVF AVTFGMNASD KTAGAFTQYA VATEDLSCLI PEAMSFTEAC
     SMGLAIATAG LALFQTPGLQ LSMQGGNGEA VLVSGGATAT GTMAIQFLRI AGYTPVVTCS
     PSNNALCESF GAEICFDYHS PTCGADIRVQ TGNKLRHVLD CVVDISTMKM SYDAIGSSGG
     AYVALEAIPT NIKYTRRDIC ANWLMAPSIL GTPVNKKGAY GRPSMPEHRQ FGTYLFALAE
     KWLQDGSIKH HPIEIREGGL RSIREGIDDL RRGNVHAKKL VYPLSA