FFSC4_GIBF5
ID FFSC4_GIBF5 Reviewed; 365 AA.
AC S0ECT9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Terpene cyclase 4 {ECO:0000303|PubMed:23335243};
DE EC=4.2.3.- {ECO:0000269|PubMed:23335243};
DE AltName: Full=Sesquiterpene synthase 4 {ECO:0000303|PubMed:23335243};
GN Name=Ffsc4 {ECO:0000303|PubMed:23335243}; ORFNames=FFUJ_12585;
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 sesquiterpene koraiol.
CC {ECO:0000269|PubMed:23335243}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + koraiol;
CC Xref=Rhea:RHEA:66640, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:167323, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:23335243};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66641;
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 koraiol.
CC {ECO:0000269|PubMed:23335243}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HF679030; CCT72694.1; -; Genomic_DNA.
DR AlphaFoldDB; S0ECT9; -.
DR SMR; S0ECT9; -.
DR STRING; 1279085.S0ECT9; -.
DR VEuPathDB; FungiDB:FFUJ_12585; -.
DR Proteomes; UP000016800; Chromosome 8.
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 InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..365
FT /note="Terpene cyclase 4"
FT /id="PRO_0000452516"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 118..122
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT MOTIF 260..268
FT /note="NSE motif"
FT /evidence="ECO:0000250|UniProtKB:P9WEY7"
FT MOTIF 341..348
FT /note="WxxxxxRY motif"
FT /evidence="ECO:0000250|UniProtKB:P9WEY7"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 347..348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ SEQUENCE 365 AA; 41636 MW; 779066CBD2109A51 CRC64;
MVPSLITPPP SRSGEATPQK DACLNPVNIA EPEGHWIKLP EALFSSIMAV EPEVNPLYRT
SKALSDEWLK TALRMNDKTA VIWSRLDIAY MSAICAPHAD LETLKLMNDW NGWVFAFDDP
FDEGTFANDP IKAAEEVIYT LATLDNIHPV VSPDENPLRH TLQSCWMRFR ERSSPSLQYR
WKKHLTMYCV GVLQQVGVQH RATRPTIEEY MDMRAGCVGA YPCIGLMEFA EGIDIPQNVM
DHPSMQAISR ITCDLVTLQN DLCSYRKDLI QGEESNIIFI LKDQGMTDQQ AVDQIGEMLY
DCYRRWHMAL ANLPFWGEGI DRDVIKFVTG CRNIALGNLH WSLYTFRYLG NDGPEVKRTR
MMKLP
