FFSC6_GIBF5
ID FFSC6_GIBF5 Reviewed; 371 AA.
AC S0EGZ9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Terpene cyclase 6 {ECO:0000303|PubMed:23335243};
DE EC=4.2.3.- {ECO:0000269|PubMed:23335243};
DE AltName: Full=Sesquiterpene synthase 6 {ECO:0000303|PubMed:23335243};
GN Name=Ffsc6 {ECO:0000303|PubMed:23335243}; ORFNames=FFUJ_10353;
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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23335243; DOI=10.1002/cbic.201200695;
RA Brock N.L., Huss K., Tudzynski B., Dickschat J.S.;
RT "Genetic dissection of sesquiterpene biosynthesis by Fusarium fujikuroi.";
RL ChemBioChem 14:311-315(2013).
CC -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl
CC diphosphate (FPP) to the spirocyclic sesquiterpene alpha-acorenol.
CC {ECO:0000269|PubMed:23335243}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (-)-alpha-acorenol +
CC diphosphate; Xref=Rhea:RHEA:66636, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:167324, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:23335243};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66637;
CC Evidence={ECO:0000269|PubMed:23335243};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UR08};
CC Note=Binds 3 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:Q9UR08};
CC -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:23335243}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UR08}.
CC -!- DOMAIN: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are
CC required for coordinating the divalent metal ions that stabilize the
CC PPi moiety of the substrate. {ECO:0000250|UniProtKB:Q9UR08}.
CC -!- DOMAIN: The C-terminal WxxxxxRY motif is frequently found in terpene
CC synthases and is important to guide product formation.
CC {ECO:0000250|UniProtKB:P9WEY7}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of the spirocyclic
CC sesquiterpene alpha-acorenol. {ECO:0000269|PubMed:23335243}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HF679032; CCT74306.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EGZ9; -.
DR SMR; S0EGZ9; -.
DR VEuPathDB; FungiDB:FFUJ_10353; -.
DR Proteomes; UP000016800; Chromosome 10.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..371
FT /note="Terpene cyclase 6"
FT /id="PRO_0000452517"
FT MOTIF 144..148
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT MOTIF 266..274
FT /note="NSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT MOTIF 352..359
FT /note="WxxxxxRY motif"
FT /evidence="ECO:0000250|UniProtKB:P9WEY7"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 358..359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ SEQUENCE 371 AA; 42495 MW; 456767A614BA1ECD CRC64;
MPHKDLPIRP LVRAFDPVGP DTLGPPDLDF ASLFRERNVP EDAPLTLYPE QLNVPWHTSL
PWTRQSKWWV QGEAAGRDLV NRISADKASE RGALPVEFMD ERRKGKIDEL VEDAVSCAVY
LYPSSSPTRI ELLTQALLLL FFHDDVMERG ATQDDATVCD DFVTMIPKNK HMKRYFAEVL
ECDPILGPGL LRAIGLFVNA GRKKSPFKQD KYATLAEYLD YRRHDIAKPF MIAAIRFGSG
VRQTPEETAP FAELEDLYVQ HSILINDLYS YDKEMYEART INGSVVNAVH VIEKLMCVPP
HLAKTITRTM SFDVEKKYYA ESERFMRDPA LNDKQRTYVI ALFDCLTGNL FHHATLGRYS
RYAEYVFDCK T
