EREMS_GIBF5
ID EREMS_GIBF5 Reviewed; 357 AA.
AC S0DX56;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=(+)-eremophilene synthase {ECO:0000303|PubMed:27294564};
DE EC=4.2.3.164 {ECO:0000269|PubMed:27294564};
DE AltName: Full=Sesquiterpene cyclase {ECO:0000303|PubMed:27294564};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:27294564};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:27294564};
GN Name=STC3 {ECO:0000303|PubMed:27294564};
GN ORFNames=FFUJ_04067 {ECO:0000312|EMBL:CCT65043.1};
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, SUBSTRATE SPECIFICITY, DOMAIN, AND REACTION
RP MECHANISM.
RX PubMed=27294564; DOI=10.1002/anie.201603782;
RA Burkhardt I., Siemon T., Henrot M., Studt L., Roesler S., Tudzynski B.,
RA Christmann M., Dickschat J.S.;
RT "Mechanistic characterisation of two sesquiterpene cyclases from the plant
RT pathogenic fungus Fusarium fujikuroi.";
RL Angew. Chem. Int. Ed. 55:8748-8751(2016).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield the bicyclic sesquiterpene eremophilene via a 1,10-
CC cyclization, which requires the abstraction of the pyrophosphate from
CC FPP to yield the (E,E)-germacradienyl cation. The only accepted
CC substrate is farnesyl diphosphate (FPP). {ECO:0000269|PubMed:27294564}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-eremophilene + diphosphate;
CC Xref=Rhea:RHEA:52804, ChEBI:CHEBI:33019, ChEBI:CHEBI:137562,
CC ChEBI:CHEBI:175763; EC=4.2.3.164;
CC Evidence={ECO:0000269|PubMed:27294564};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Glu (DDXXE) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:27294564}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HF679024; CCT65043.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DX56; -.
DR SMR; S0DX56; -.
DR STRING; 1279085.S0DX56; -.
DR EnsemblFungi; CCT65043; CCT65043; FFUJ_04067.
DR KEGG; ag:CCT65043; -.
DR VEuPathDB; FungiDB:FFUJ_04067; -.
DR HOGENOM; CLU_042538_0_1_1; -.
DR BRENDA; 4.2.3.164; 2425.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000016800; Chromosome 2.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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..357
FT /note="(+)-eremophilene synthase"
FT /id="PRO_0000443302"
FT MOTIF 100..105
FT /note="DDXXE motif"
FT /evidence="ECO:0000305|PubMed:27294564"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 331..332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 357 AA; 40971 MW; 0493E69702E14481 CRC64;
MIATINGDTK INGKGHPTEV RIPDMFGSIM SATPMVNPHH FKVKAAADAF IADYLKMDKH
EATKNRKADF CFCASAMAPH ADAEALRTMV DWLNWIFYFD DDFDEGQLDR DPVAAEKEIR
HTLAVLEEGA EIPDRELHPL RYLFRTIWDR VKERAYPDVQ TQFKITHKRY LDGLLHQVEA
TRDGNGQPRT EEDYIRMRRR TVGGYPCISL IAYAHNVDLS QEAFEHPSVQ ECIAVGCDLA
WIHNDIVSYK KDVKSGIEHN FITVLKKNGF TTQQAMDRAG ELQDECYRRW YLALASMPIW
GESIDREVLR YIEACHSFPL GDLLWSFQTG RYLGATEGYK LHETRVLDLS DLEPIAV
