FUS2_GIBM7
ID FUS2_GIBM7 Reviewed; 419 AA.
AC W7N6P0;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=20-hydroxy-prefusarin hydrolase FUS2 {ECO:0000250|UniProtKB:S0EE80};
DE EC=3.7.1.- {ECO:0000250|UniProtKB:S0EE80};
DE AltName: Full=Fusarin biosynthesis protein 2 {ECO:0000303|PubMed:22652150};
GN Name=FUS2 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11085;
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: 20-hydroxy-prefusarin hydrolase; part of the gene cluster
CC that mediates the biosynthesis of the mycotoxin fusarin C
CC (PubMed:17121404, PubMed:22652150). Within the cluster, FUS1, FUS2,
CC FUS8 and FUS9 are sufficient for fusarin production (By similarity).
CC The roles of the other FUS members are yet undetermined (By
CC similarity). The fusarin C synthetase FUS1 is responsible for the
CC condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA
CC units and the amide linkage of the arising heptaketide and homoserine,
CC subsequently releasing the first intermediate, prefusarin, as an
CC alcohol with an open ring structure (PubMed:17121404). The cytochrome
CC P450 monooxygenase FUS8 participates in multiple oxidation processes at
CC carbon C-20 and is able to use the FUS1 product as substrate, resulting
CC in formation of 20-hydroxy-prefusarin (By similarity). This reaction
CC seems to be essential before the 2-pyrrolidone ring closure can be
CC catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8
CC is able to further oxidizes carbon C-20 after ring closure, resulting
CC in the formation of carboxy-fusarin C (By similarity). As the last
CC step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C
CC (By similarity). Fusarin C can then rearrange to epi-fusarin C, the
CC (z)-isomers, and fusarin A and fusarin D (By similarity).
CC {ECO:0000250|UniProtKB:S0EE80, ECO:0000269|PubMed:17121404,
CC ECO:0000269|PubMed:22652150}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:S0EE80,
CC ECO:0000305|PubMed:22652150}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase
CC family. {ECO:0000305}.
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DR EMBL; DS022257; EWG52307.1; -; Genomic_DNA.
DR RefSeq; XP_018758498.1; XM_018900248.1.
DR AlphaFoldDB; W7N6P0; -.
DR SMR; W7N6P0; -.
DR EnsemblFungi; FVEG_11085T0; FVEG_11085T0; FVEG_11085.
DR GeneID; 30068621; -.
DR KEGG; fvr:FVEG_11085; -.
DR VEuPathDB; FungiDB:FVEG_11085; -.
DR eggNOG; ENOG502QPTG; Eukaryota.
DR HOGENOM; CLU_034451_0_0_1; -.
DR OMA; EELYFYG; -.
DR OrthoDB; 1133794at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010520; FrsA-like.
DR Pfam; PF06500; FrsA-like; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..419
FT /note="20-hydroxy-prefusarin hydrolase FUS2"
FT /id="PRO_0000437358"
FT ACT_SITE 238
FT /evidence="ECO:0000250|UniProtKB:Q93NG6"
SQ SEQUENCE 419 AA; 46314 MW; 3F1059F1C0EAF61B CRC64;
MHKVFASDFF NFEFLRLLGT VPFQGAEVGE CLTTAGRIKD GDPESWYRAW RDQAEKAQAL
AEEAAAVGDR TGACWAYIRA ANYWRASEFL LHCTPNDPRI LAASKASVNA FDKGWVLLDA
TVKSFEIPYD KDIKLPGRLY LPAPHHRLPG KIPVVLQTGG FDSTQEELYF YGAAGALPRG
YAVFSFDGPG QGLPLRVGKL KLRTDWEYVV SQVLDFVTDD IAPEYDLDLE RLAIFGASLG
GYLSLRAAVD PRIKACISCD GPLDLFEITR SRMPSWFING WLSGWVSDGL FNWVVDALTA
VNFQIAWEFG HGKWVFGVET PADVLRVMQQ ISLKGGYLSK IKCPTLITGA ADSFYFTPDI
NANPIFEGLT ALGSNEKHLW IGKGVEGGGL QAKIGALAVV HHKMFTWLDS TFAIKRDVL
