CGDS_COLGL
ID CGDS_COLGL Reviewed; 744 AA.
AC P9WEV7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Dolasta-1(15),8-diene synthase {ECO:0000303|PubMed:30277637};
DE Short=DS {ECO:0000303|PubMed:30277637};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:30277637};
DE EC=4.2.3.- {ECO:0000269|PubMed:30277637};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:30277637};
DE Short=GGDP synthase {ECO:0000303|PubMed:30277637};
DE Short=GGS {ECO:0000303|PubMed:30277637};
DE EC=2.5.1.29 {ECO:0000269|PubMed:30277637};
GN Name=CgDS {ECO:0000303|PubMed:30277637};
OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=474922;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP DOMAIN.
RX PubMed=30277637; DOI=10.1002/anie.201809954;
RA Bian G., Rinkel J., Wang Z., Lauterbach L., Hou A., Yuan Y., Deng Z.,
RA Liu T., Dickschat J.S.;
RT "A clade II-D fungal chimeric diterpene synthase from Colletotrichum
RT gloeosporioides produces dolasta-1(15),8-diene.";
RL Angew. Chem. Int. Ed. 57:15887-15890(2018).
CC -!- FUNCTION: Bifunctional terpene synthase involved in the biosynthesis of
CC the diterpene dolasta-1(15),8-diene (PubMed:30277637). The C-terminal
CC prenyltransferase domain of CgDS catalyzes formation of the universal
CC precursor of diterpene, geranylgeranyl diphosphate (GGPP), whereas the
CC N-terminal terpene cyclase domain catalyzes the cyclization of GGPP to
CC dolasta-1(15),8-diene (PubMed:30277637). {ECO:0000269|PubMed:30277637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:30277637};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30277637};
CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}.
CC -!- DOMAIN: The DDXXD motifs are important for the catalytic activity,
CC presumably through binding to Mg(2+). {ECO:0000305|PubMed:30277637}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P9WEV7; -.
DR SMR; P9WEV7; -.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 2.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Repeat; Transferase.
FT CHAIN 1..744
FT /note="Dolasta-1(15),8-diene synthase"
FT /id="PRO_0000450828"
FT REGION 1..344
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:30277637"
FT REGION 345..744
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:30277637"
FT REGION 399..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..112
FT /note="DDXXD"
FT /evidence="ECO:0000305|PubMed:30277637"
FT MOTIF 495..499
FT /note="DDXXD"
FT /evidence="ECO:0000305|PubMed:30277637"
FT COMPBIAS 407..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 198..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 246..250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 336..337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 459
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 488
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 504
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 505
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 581
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 582
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 617
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 744 AA; 83696 MW; 72DBEAF6F7F03F3B CRC64;
MASTMMNYQD CGPMRYKSSV PVPASLYENT AYPSKFRPRI SKHVDVADKA CWEACDDFEN
ATGLKLKADS VGCINPIGGN VNALWFPEAI PERLHIISYL SELLFRHDDL TDDAVTPEQF
DEVHGPLARF LGSESKQSDH TTKHNAMNTM QARVAIEALE QNEQLGKLVI EKWKGIVSVR
GQDAFMEHKT LDSYMHVRHY DAGAYSVWSQ ILFCCDISLT DEELTGLEPL TWLAFTQMIL
WHDYCSWDKE AATYLEREEG GSNMSAVQVY MAMYGLDQYA AKEFLLSEIT RIEDEYCERK
ASYMIEFPPA PHITHYIGLI EMCMAGNTLW HLSSRRYNPA APLPRREDIG KVNGGPLDAS
EVSKPVECSE SDLGILTPVS SRLSTKRLRP FWNNQRTEYT TMTPAETSSD DKKKKAKASH
ETREDLLTVS PCAWPAEPDE KDILAAYLYT AARPASGARD KLMDALDKWY RVPPDALATI
RTIIRIMHNA SLMLDDVQDN SPVRRGSPSA HVIFGTAQTT NSASYLMIKC VDLARRLGDD
SLSCLLSELS QLHLGQSHDL AWTFHCKAPS IPEYYSHLEQ KTGGLFRMAS RMMRASATQN
KHLDACKLMS LLGRLYQLRD DYQDITSESL STYDDLDEGS FTLPLIHALH REEEQGEVQL
HSILQSARAA RSASASSNND GKLSVETKLL IREMLEEAGS LEHTRVVIRG LYDETRAVLT
AMENEAGSGG KNWMLHLITF QLKV
