FUS8_GIBM7
ID FUS8_GIBM7 Reviewed; 514 AA.
AC W7MLD1;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Cytochrome P450 monooxygenase FUS8 {ECO:0000303|PubMed:22652150};
DE EC=1.-.-.- {ECO:0000250|UniProtKB:S0EE84};
DE AltName: Full=Fusarin biosynthesis protein 8 {ECO:0000303|PubMed:22652150};
GN Name=FUS8 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11079;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2]
RP FUNCTION.
RX PubMed=17121404; DOI=10.1002/cbic.200600404;
RA Rees D.O., Bushby N., Cox R.J., Harding J.R., Simpson T.J., Willis C.L.;
RT "Synthesis of [1,2-13C2, 15N]-L-homoserine and its incorporation by the
RT PKS-NRPS system of Fusarium moniliforme into the mycotoxin fusarin C.";
RL ChemBioChem 8:46-50(2007).
RN [3]
RP FUNCTION.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxin fusarin C (PubMed:17121404,
CC PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC sufficient for fusarin production (By similarity). The roles of the
CC other FUS members are yet undetermined (By similarity). 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:17121404). 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 (By similarity). This reaction seems to be essential
CC before the 2-pyrrolidone ring closure can be catalyzed by FUS2,
CC generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further
CC oxidizes carbon C-20 after ring closure, resulting in the formation of
CC carboxy-fusarin C (By similarity). As the last step, FUS9 methylates
CC the hydroxyl group at C-21 to generate fusarin C (By similarity).
CC Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and
CC fusarin A and fusarin D (By similarity). {ECO:0000250|UniProtKB:S0EE84,
CC ECO:0000269|PubMed:17121404, ECO:0000269|PubMed:22652150}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:S0EE84,
CC ECO:0000305|PubMed:22652150}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DS022257; EWG52298.1; -; Genomic_DNA.
DR RefSeq; XP_018758489.1; XM_018900239.1.
DR AlphaFoldDB; W7MLD1; -.
DR SMR; W7MLD1; -.
DR STRING; 117187.FVEG_11079T0; -.
DR EnsemblFungi; FVEG_11079T0; FVEG_11079T0; FVEG_11079.
DR GeneID; 30068615; -.
DR KEGG; fvr:FVEG_11079; -.
DR VEuPathDB; FungiDB:FVEG_11079; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_4_1_1; -.
DR OMA; MFGIRYI; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000009096; 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 3: Inferred from homology;
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_0000437364"
FT TRANSMEM 28..48
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; 58272 MW; 6177FFE783ADE4D9 CRC64;
MESTPLQYPL GLKTDSLVKQ VSEVLKSLTV TKAVGAFIVL FIIIPKVFDF LRNLFSPVTS
IPGPLINKFS PWPLEIATFK GKSHRFARAL HRKYGPIVVL APGMISIGDS KEIKRIIQSE
DWVKSEAIYG NFRQDFHRPT LLAFTEKKAY SRRKRMLSSM FGIRYIRSLE PLMKSCVDAG
VAHLNKLCDN PSKSTIINLQ HFIHGLAIDT IGVTTFGGSF HVVENGSHPL PSRLKAGMKI
SAVMQLISWI KYIPFLPKRD PYIEKFTFDI VDKRRKEAGA VKHQDLLQHL VDVCDDSPGS
EFRTSDVQDE SVILLAAGSE TTANAELFTV IQLLKHPEKM KKLIAEVDKW YPPSEPDRAT
ECAYSQTGMT YLQACIDETM RLIPGQATGS PREASKQEVL LGYKIPRGTT VFPNTQEAHL
DGSIWEQPEK YIPERWLEIY SRNQTSAMPY WPFSAGSRIC VGKNFAFQEM HISLTTLLRK
FTFEYVPGQD ETTVFRIAQQ LEADSYKVRV KKRF
