GUDIS_GIBF5
ID GUDIS_GIBF5 Reviewed; 401 AA.
AC S0ENM8;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Inactive (1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase {ECO:0000305|PubMed:27294564};
GN Name=STC5 {ECO:0000303|PubMed:27294564};
GN ORFNames=FFUJ_11739 {ECO:0000312|EMBL:CCT75704.1};
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 MUTAGENESIS OF LYS-288, AND DOMAIN.
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 -!- 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 -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp (DDXXD) 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}.
CC -!- CAUTION: Although similar to (1R,4R,5S)-(-)-guaia-6,10(14)-diene
CC synthase, lacks the metal binding site Asn at position 288 and does not
CC show (1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase activity. Converting
CC Lys-288 to a asparagine restores activity.
CC {ECO:0000269|PubMed:27294564}.
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DR EMBL; HF679033; CCT75704.1; -; Genomic_DNA.
DR AlphaFoldDB; S0ENM8; -.
DR SMR; S0ENM8; -.
DR STRING; 1279085.S0ENM8; -.
DR EnsemblFungi; CCT75704; CCT75704; FFUJ_11739.
DR KEGG; ag:CCT75704; -.
DR VEuPathDB; FungiDB:FFUJ_11739; -.
DR HOGENOM; CLU_042538_0_1_1; -.
DR BRENDA; 4.2.3.165; 2425.
DR Proteomes; UP000016800; Chromosome 11.
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 Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..401
FT /note="Inactive (1R,4R,5S)-(-)-guaia-6,10(14)-diene
FT synthase"
FT /id="PRO_0000443321"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..138
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27294564"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 375..376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT MUTAGEN 288
FT /note="K->N: Restores (1R,4R,5S)-(-)-guaia-6,10(14)-diene
FT synthase activity."
FT /evidence="ECO:0000269|PubMed:27294564"
SQ SEQUENCE 401 AA; 45986 MW; 95AA657CB9CA63E1 CRC64;
MVKFDSGSES EMTNGDELHI NSKHEVKSRM ANGNGVHNVP DHDQFQDRAE MEVLILPDLF
SSLMSVPARE NPHYASVKAD ADEWISFVIN ADAKWASRNK RVDFTYLASI WAPDCSAFAL
RTSADWNSWA FLFDDQFDEG HLSNDLEGAI NEIARTREIM EGTAPRYTAD SEHPIRYVFQ
TLCDRVKQNP EGFYAGKPSS ERFYRRWMWA HELYWEGLVA QVRTNVEGRS FTRGPEEYLA
MRRGSLGAYP ALVNNEWAYG IDLPEEVADH PLVFEIMIIM SDQILLVKDI LSYEKDLRLG
VDHNMVRLLK AKGLSTQQAI NEVGVMINNC YRRYYRALSE LPCFGEEADR ALLGYLEVEK
NHALGSLLWS YNTGRYFKSK EDGARVRKTR ELLIPKKMAA L
