FSR4_GIBF5
ID FSR4_GIBF5 Reviewed; 338 AA.
AC S0DQ98; G8C422;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Trans-enoyl reductase fsr4 {ECO:0000303|PubMed:22492438};
DE EC=1.-.-.- {ECO:0000305|PubMed:22492438};
DE AltName: Full=Fusarubin biosynthesis cluster protein 4 {ECO:0000303|PubMed:22492438};
GN Name=fsr4 {ECO:0000303|PubMed:22492438}; ORFNames=FFUJ_03987;
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 [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=22492438; DOI=10.1128/aem.00823-12;
RA Studt L., Wiemann P., Kleigrewe K., Humpf H.U., Tudzynski B.;
RT "Biosynthesis of fusarubins accounts for pigmentation of Fusarium fujikuroi
RT perithecia.";
RL Appl. Environ. Microbiol. 78:4468-4480(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
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).
CC -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of fusarubins, highly pigmented naphthoquinones
CC responsible for the coloration of the fruiting bodies (PubMed:22492438,
CC PubMed:23825955). The non-reducing polyketide synthase FSR1 is
CC responsible for the condensation of seven acetyl-CoA units to yield a
CC haptaketide (PubMed:22492438). After rings A and B are formed by aldol-
CC type cyclization, the PKS-derived product is released as 6-O-
CC demethylfusarubinaldehyde (PubMed:22492438). Then, two hydroxyl groups
CC at C-5 and C-10 are incorporated by FSR3, and simultaneously hydroxyl
CC groups at C-6 and C-8 are methylated by FSR2 (PubMed:22492438). The
CC aldehyde is, on the one hand, reduced by FSR3 to 8-O-methylfusarubin
CC alcohol, which equilibrates mainly with 8-O-methylfusarubin and only
CC small amounts of 8-O-methylnectriafurone (PubMed:22492438). On the
CC other hand, the aldehyde can be oxidized to form 8-O-methylfusarubinic
CC acid, a reaction driven by FSR3 equilibrating with 8-O-
CC methylfusarubinlactone, finally resulting in 8-O-
CC methylanhydrofusarubinlactol after a further reduction step and loss of
CC water (PubMed:22492438). 8-O-Methylfusarubinic acid can also undergo
CC decarboxylation, resulting in 8-O-methyl-13-hydroxynorjavanicin after
CC another hydroxylation step at C-13 (PubMed:22492438). Both steps are
CC most likely also accomplished by FSR3 (PubMed:22492438). No enzymatic
CC function has been determined so far for either FSR4 and FSR5
CC (PubMed:22492438). Their deletion does not alter the product spectrum,
CC but the possibility that they catalyze specific enzymatic steps during
CC perithecium development cannot be ruled out (PubMed:22492438). FSR4
CC might possess a regulatory function in the biosynthesis of fusarubins
CC (PubMed:22492438). {ECO:0000269|PubMed:22492438,
CC ECO:0000269|PubMed:23825955}.
CC -!- INDUCTION: Expression is induced in presence of sodium nitrate, and
CC repressed by glutamine (PubMed:22492438).
CC {ECO:0000269|PubMed:22492438}.
CC -!- DISRUPTION PHENOTYPE: Leads to an enriched product formation
CC (PubMed:22492438). {ECO:0000269|PubMed:22492438}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; HE613440; CCE67073.1; -; Genomic_DNA.
DR EMBL; HF679024; CCT64759.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DQ98; -.
DR SMR; S0DQ98; -.
DR STRING; 1279085.S0DQ98; -.
DR EnsemblFungi; CCT64759; CCT64759; FFUJ_03987.
DR EnsemblFungi; KLP16368; KLP16368; LW94_5851.
DR VEuPathDB; FungiDB:FFUJ_03987; -.
DR Proteomes; UP000016800; Chromosome 2.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 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..338
FT /note="Trans-enoyl reductase fsr4"
FT /id="PRO_0000442027"
FT BINDING 65..68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 147..153
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 182..185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 205..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 277..278
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 338 AA; 36985 MW; 5F344AA70715555E CRC64;
MFSHLRNRLS VNRPQALSSQ IRAASTMKEA IVSRGPRVHI IDSPIPKAGP GQVVVKIEYA
GSNPKDWKRP EYWGSKATMN QGDDHSGTVY EVGEGVSDFK IGDRVAAMHE GKQPGGSYAE
YGVSWAYTTI HLPEQTTFQE GAAIPFAAFT AACALYAKLD LPYPRHPVSD DQKIPLVIWG
ASSAVGSYAV QLAKKSNIHP LICIAGRAQE HVERMIDGSK GDIVIDYRKG HEAVAQKIKA
NLSGQKLEYA FDAVSEMGSY QTICDVLDQE IGKITLIIPA QSYSDIPKTI KKSVTTVASV
HEDLKEFARG FSTYFGRGLQ DGWLKAHPQE VVPGDWRG
