FUS2_GIBF5
ID FUS2_GIBF5 Reviewed; 419 AA.
AC S0EE80;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=20-hydroxy-prefusarin hydrolase FUS2 {ECO:0000303|PubMed:23932525};
DE EC=3.7.1.- {ECO:0000305|PubMed:23932525};
DE AltName: Full=Fusarin biosynthesis protein 2 {ECO:0000303|PubMed:23932525};
GN Name=FUS2 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10057;
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: 20-hydroxy-prefusarin hydrolase; part of the gene cluster
CC that mediates the biosynthesis of the mycotoxin fusarin C
CC (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC sufficient for fusarin production (PubMed:23932525). The roles of the
CC other FUS 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23932525}.
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-prefusarin
CC (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase
CC family. {ECO:0000305}.
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DR EMBL; HF679031; CCT73261.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EE80; -.
DR SMR; S0EE80; -.
DR ESTHER; gibf5-fus2; Duf_1100-S.
DR EnsemblFungi; CCT73261; CCT73261; FFUJ_10057.
DR VEuPathDB; FungiDB:FFUJ_10057; -.
DR HOGENOM; CLU_034451_0_0_1; -.
DR BioCyc; MetaCyc:MON-19359; -.
DR Proteomes; UP000016800; 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 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..419
FT /note="20-hydroxy-prefusarin hydrolase FUS2"
FT /id="PRO_0000437357"
FT ACT_SITE 238
FT /evidence="ECO:0000250|UniProtKB:Q93NG6"
SQ SEQUENCE 419 AA; 46437 MW; 3076A5D1BF7665D3 CRC64;
MHKVFASDFF NFEFLRLLGT VPFQGAEVGE CLTTAGRIKD GDPESWYRAW RDQAEKAQAL
AEEAAAVGDK TGACWAYIRA ANYWRASEFL LHCTPKDPRI LASSKASVNA FDKGWVLLDA
TVKNFEIPYE KDIKLPGRLY LPAPHHRLPG KIPVVLQTGG FDSTQEELYF YGAAGALPRG
YAVFSFDGPG QGLPLRVGKL KLRTDWEYVV SQVLDFVTDD VAPEYDLDLE RLAIFGASLG
GYLSLRAAVD PRIKACVSCD GPLDLFEITR SRMPPWFING WLSGWVSDGV FNWVVDGLTA
VNFQIAWEFG HGKWVFGVET PADVLRVMQK ISLKGGYLEK IKCPTLITGA ADSFYFTPDI
NANIIFEGLT ALEPNDKHLW IGKGVEGGGL QAKIGALAVV HHKMFTWLDS TFAIKRDVL
