FSR5_GIBF5
ID FSR5_GIBF5 Reviewed; 265 AA.
AC S0DRI2; G8C423;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Short-chain dehydrogenase/reductase fsr5 {ECO:0000303|PubMed:22492438};
DE EC=1.1.-.- {ECO:0000305|PubMed:22492438};
DE AltName: Full=Fusarubin biosynthesis cluster protein 35 {ECO:0000303|PubMed:22492438};
DE Flags: Precursor;
GN Name=fsr5 {ECO:0000303|PubMed:22492438}; ORFNames=FFUJ_03988;
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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that 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 -!- INDUCTION: Expression is induced in presence of sodium nitrate, and
CC repressed by glutamine (PubMed:22492438).
CC {ECO:0000269|PubMed:22492438}.
CC -!- DISRUPTION PHENOTYPE: Does nor affect the production of the fusarubins
CC (PubMed:22492438). {ECO:0000269|PubMed:22492438}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCE67074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE613440; CCE67074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HF679024; CCT65046.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DRI2; -.
DR SMR; S0DRI2; -.
DR EnsemblFungi; CCT65046; CCT65046; FFUJ_03988.
DR VEuPathDB; FungiDB:FFUJ_03988; -.
DR HOGENOM; CLU_010194_15_2_1; -.
DR Proteomes; UP000016800; Chromosome 2.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; NADP; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..265
FT /note="Short-chain dehydrogenase/reductase fsr5"
FT /id="PRO_0000442028"
FT BINDING 17..41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 265 AA; 28074 MW; D3768DE9E7EAF7EC CRC64;
MASLGKYVSK LAGSRVLVIG GSSGIGFGVA EAAIQNGASS VFISSSSQTK ISSAIERLKE
NNQSAKAQLH GFPCNLGSPD TLTSEVENLF AEVAKSGKLD HVVFTAGDKL AVGKLEDFTL
DAIRQAGTVR FFAPLVVAQQ LRKHLDESGS SSFTVATGGA TEHVSKDWSI MYSYLSGLRG
MIRGLAVDLA PIRVNAVAQG PTDTEIWSYV KEMGYWDNVT GHLKGRMTTG EIGKVEDVVE
AYLYLMKNKN TSGSVVETTG GTLLS
