FSR3_GIBF5
ID FSR3_GIBF5 Reviewed; 522 AA.
AC S0DQN6; G8C421;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=FAD-dependent monooxygenase fsr3 {ECO:0000303|PubMed:22492438};
DE EC=1.-.-.- {ECO:0000269|PubMed:22492438};
DE AltName: Full=Fusarubin biosynthesis cluster protein 3 {ECO:0000303|PubMed:22492438};
GN Name=fsr3 {ECO:0000303|PubMed:22492438}; ORFNames=FFUJ_03986;
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, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
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: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of fusarubins, highly pigmented
CC naphthoquinones responsible for the coloration of the fruiting bodies
CC (PubMed:22492438, PubMed:23825955). The non-reducing polyketide
CC synthase FSR1 is responsible for the condensation of seven acetyl-CoA
CC units to yield a haptaketide (PubMed:22492438). After rings A and B are
CC formed by aldol-type cyclization, the PKS-derived product is released
CC as 6-O-demethylfusarubinaldehyde (PubMed:22492438). Then, two hydroxyl
CC groups at C-5 and C-10 are incorporated by FSR3, and simultaneously
CC hydroxyl groups at C-6 and C-8 are methylated by FSR2
CC (PubMed:22492438). The aldehyde is, on the one hand, reduced by FSR3 to
CC 8-O-methylfusarubin alcohol, which equilibrates mainly with 8-O-
CC methylfusarubin and only small amounts of 8-O-methylnectriafurone
CC (PubMed:22492438). On the other hand, the aldehyde can be oxidized to
CC form 8-O-methylfusarubinic acid, a reaction driven by FSR3
CC equilibrating with 8-O-methylfusarubinlactone, finally resulting in 8-
CC O-methylanhydrofusarubinlactol after a further reduction step and loss
CC of 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:22492438}.
CC -!- INDUCTION: Expression is repressed under acidic conditions, while the
CC expression is induced under alkaline conditions (PubMed:22492438).
CC Expression is induced in presence of sodium nitrate, and repressed by
CC glutamine (PubMed:22492438). {ECO:0000269|PubMed:22492438}.
CC -!- DISRUPTION PHENOTYPE: Leads to an alteration in the product spectrum,
CC with an accumulation of fusarubinaldehyde (PubMed:22492438).
CC {ECO:0000269|PubMed:22492438}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; HE613440; CCE67072.1; -; Genomic_DNA.
DR EMBL; HF679024; CCT64760.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DQN6; -.
DR SMR; S0DQN6; -.
DR STRING; 5127.CCT64760; -.
DR EnsemblFungi; CCT64760; CCT64760; FFUJ_03986.
DR EnsemblFungi; KLP16367; KLP16367; LW94_5850.
DR VEuPathDB; FungiDB:FFUJ_03986; -.
DR Proteomes; UP000016800; Chromosome 2.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..522
FT /note="FAD-dependent monooxygenase fsr3"
FT /id="PRO_0000442026"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 85..86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 379..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 522 AA; 58721 MW; 502D88BC11CC9FEB CRC64;
MKNTQTNGTH PIIDKKPNGT LNGDHQEYPT FSQEKLDDSI KRGIDLQVFR YPSTGINVLI
AGAGLGGITC ALECWRKGHN VRIIDRSPSP VWTGDNVQIQ PSAILLLRHW PDMGYEIEEN
QYDVDMSYYR QTGERIWGPA PPMFNDPEHL PGRRGFPSVN AHSRIKLYRA FLKQAERVGI
YVEWGCKVVE YWEDVEGHAG GVVLENGEKR TADIVVAADG LRTKSMTIVP GMPDQLTTSG
KAIYRAGYPV EHALKDPTVR EMWNFKPEDK PIWQFWLGNG SHNMMCLTHD LAFWSFIHSH
AESASESWIP DIDPAEVITE MEKNDAVHPA IAALIRTAPK GSVVNWQLKF RDPHEQWTSP
GGHVVQLGDA AHAFLPTSGN GATQAIEDGV TLATCLQLAG KAQAANATKV YNKLRFQRVS
CGQKMGFVNQ QLKQHTDWDA IMKNPALIRS RYPKWVWSHD PEAYAYEKFA EALTHVVSGG
RVPLVNTNFP KGHKYRHWTM KEVQEQIKAG QKLEDLQDGD WS
