FUS8_GIBF5
ID FUS8_GIBF5 Reviewed; 514 AA.
AC S0EE84;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome P450 monooxygenase FUS8 {ECO:0000303|PubMed:23932525};
DE EC=1.-.-.- {ECO:0000305|PubMed:23932525};
DE AltName: Full=Fusarin biosynthesis protein 8 {ECO:0000303|PubMed:23932525};
GN Name=FUS8 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10051;
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 INDUCTION.
RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA Tudzynski B.;
RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL Mol. Microbiol. 77:972-994(2010).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT insight into the complex regulation and fusarin biosynthetic pathway.";
RL Chem. Biol. 20:1055-1066(2013).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxin fusarin C (PubMed:23932525).
CC Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for
CC fusarin production (PubMed:23932525). The roles of the other FUS
CC members are yet undetermined (PubMed:23932525). The fusarin C
CC synthetase FUS1 is responsible for the condensation of one acetyl-
CC coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage
CC of the arising heptaketide and homoserine, subsequently releasing the
CC first intermediate, prefusarin, as an alcohol with an open ring
CC structure (PubMed:23932525). The cytochrome P450 monooxygenase FUS8
CC participates in multiple oxidation processes at carbon C-20 and is able
CC to use the FUS1 product as substrate, resulting in formation of 20-
CC hydroxy-prefusarin (PubMed:23932525). This reaction seems to be
CC essential before the 2-pyrrolidone ring closure can be catalyzed by
CC FUS2, generating 20-hydroxy-fusarin (PubMed:23932525). FUS8 is able to
CC further oxidizes carbon C-20 after ring closure, resulting in the
CC formation of carboxy-fusarin C (PubMed:23932525). As the last step,
CC FUS9 methylates the hydroxyl group at C-21 to generate fusarin C
CC (PubMed:23932525). Fusarin C can then rearrange to epi-fusarin C, the
CC (z)-isomers, and fusarin A and fusarin D (PubMed:23932525).
CC {ECO:0000269|PubMed:23932525}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23932525}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC GLN1 (PubMed:23932525). Moreover, components of the fungal-specific
CC velvet complex VEL1, VEL2 and LAE1 act also as positive regulators of
CC expression (PubMed:20572938, PubMed:23932525). Finally, expression is
CC induced under acidic conditions in a PACC-independent manner
CC (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:23932525}.
CC -!- DISRUPTION PHENOTYPE: Accumulates 20-hydroxy-fusarin (PubMed:23932525).
CC {ECO:0000269|PubMed:23932525}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {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; HF679031; CCT73266.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EE84; -.
DR SMR; S0EE84; -.
DR STRING; 1279085.S0EE84; -.
DR EnsemblFungi; CCT73266; CCT73266; FFUJ_10051.
DR VEuPathDB; FungiDB:FFUJ_10051; -.
DR HOGENOM; CLU_001570_4_1_1; -.
DR BioCyc; MetaCyc:MON-19358; -.
DR Proteomes; UP000016800; Chromosome 9.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..514
FT /note="Cytochrome P450 monooxygenase FUS8"
FT /id="PRO_0000437363"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 460
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 514 AA; 58312 MW; 948B172CB4EF5BA3 CRC64;
MDSKPLEYLL GLNSDGSVKK VSEVFENLTV TNTVCAFIAL FIIVPRVFDF LRNLFSPVIS
IPGPLINKFS PWPLEIATFK GKSHRFARAL HRKYGPIVVL APGMISIGDS QEIKRIIQSE
DWAKSEAIYG NFRQDFHRPT LLAFTEKKAY SRRKRMLSSM FGIRYIRSLE PLMKSCVDAG
VAHLNKLCDN PSKSTVINLQ HFIHGLAIDT IGVTTFGGSF HVVENGSHPL PSRLKAGMKI
SAVMQLIGWI KYIPFLPKRD PYIEKFTFDI VDKRRKEAGA VKYQDLLQHL VDVCDDSPGS
EFRTSDVQDE SVILLAAGSE TTANAELFTV IQLLKHPEVM KKLIAEVDKW YPPSEPDRVT
ECAYSQTGMT YLQACIDETM RLIPGQATGS PRETSKQESL LGYKIPRGTT VFPNTQEAHL
DGSIWEQPEK YIPERWLEIY SQNQTSAMPY WPFSAGSRIC VGKNFAFQEM HISLTTLLRK
FTFEYVPGQD ETTVFRIAQQ LETDSYKVRV KKRF
