EVVS_EMEVA
ID EVVS_EMEVA Reviewed; 705 AA.
AC A0A0P0ZD79;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Variediene synthase {ECO:0000303|PubMed:26546087};
DE Short=VS {ECO:0000303|PubMed:26546087};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:26546087};
DE EC=4.2.3.- {ECO:0000269|PubMed:26546087};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:26546087};
DE Short=GGDP synthase {ECO:0000303|PubMed:26546087};
DE Short=GGS {ECO:0000303|PubMed:26546087};
DE EC=2.5.1.29 {ECO:0000269|PubMed:26546087};
GN Name=EvVS {ECO:0000303|PubMed:26546087};
OS Emericella variicolor (Aspergillus stellatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1549217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
RP AND PATHWAY.
RC STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX PubMed=26546087; DOI=10.1002/anie.201509263;
RA Qin B., Matsuda Y., Mori T., Okada M., Quan Z., Mitsuhashi T., Wakimoto T.,
RA Abe I.;
RT "An unusual chimeric diterpene synthase from Emericella variecolor and its
RT functional conversion into a sesterterpene synthase by domain swapping.";
RL Angew. Chem. Int. Ed. 55:1658-1661(2016).
CC -!- FUNCTION: Bifunctional terpene synthase converts DMAPP and IPP, and
CC also GGPP, into variediene as a single product (PubMed:26546087). The
CC C-terminal prenyltransferase (PT) domain of EvVS catalyzes formation of
CC GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC cyclization of GGPP to variediene (PubMed:26546087). The PT domain can
CC also synthesize GFPP from the C5 isoprene units in vitro, while the TC
CC domain is able to cyclize GFPP to the sesterterpene (2E)-alpha-
CC cericerene (PubMed:26546087). {ECO:0000269|PubMed:26546087}.
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:26546087};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:26546087};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WEV7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:26546087}.
CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}.
CC -!- DOMAIN: The conserved DDXXD motifs as well as the NSE/DTE motif are
CC important for the catalytic activity, presumably through binding to
CC Mg(2+). {ECO:0000305|PubMed:26546087}.
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 EMBL; LC063849; BAT32888.1; -; Genomic_DNA.
DR SMR; A0A0P0ZD79; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
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..705
FT /note="Variediene synthase"
FT /id="PRO_0000453637"
FT REGION 9..331
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:26546087"
FT REGION 332..705
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:26546087"
FT REGION 349..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..104
FT /note="DDXXD 1"
FT /evidence="ECO:0000305|PubMed:26546087"
FT MOTIF 230..238
FT /note="NSE/DTE"
FT /evidence="ECO:0000305|PubMed:26546087"
FT MOTIF 463..467
FT /note="DDXXD 2"
FT /evidence="ECO:0000305|PubMed:26546087"
FT COMPBIAS 349..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 186..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 234..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 325..326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 424
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 427
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 456
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 472
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 473
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 550
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 551
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 589
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 596
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 605
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 615
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 705 AA; 80309 MW; 850DA687472D61E2 CRC64;
MSQSSDFILN STLSSVVERS TPDIAGFCSG YELRRHHHEH LANEGSLRCR TDWEQFIGPI
ERWGSCNPWE GHFGAVVLPF CKPERLAVIC YIFEYAFLYD NVVESAAKST LNLNTDNIAL
DETEYRTVRS ILGTKQIQSK MLLELLSIDA PRAEVVINSW KEMISTTAKK DKTRAFNNLE
EYVDYRIIDT GAPFVDMLMR FGMGIMLTQE EQKRIEPIVK PCYAALGLAN DYFSFDIEWE
EFQAESDKTT MTNAVWLFMQ WENLNAEQAK RRVQEVTKQY EQQYLRNIAD FAAGEGKENI
KLQTYLKAQG YQVPGNVAWS LRCPRYHPWL CKEAASLLHQ DTIQELEAGR KPQALEEYRS
RSHSESDLSD ASPTFWSGSC RSSARSSVSS AFGPPDKDIS ITPAILGDEH LLGPAEYISS
LPSKGVREAF IDGLNVWLVL PDHRVNQLKS IAQTLHNASL MLDDIEDHSP LRRGRPSTHM
IFGTEQTINS ANFLLIDVME KVRQLDDPRC MDIYLEEMRN LFIGQSFDLY WTRNGECPSE
EQYLDMIRQK TGGLFRLLTR MMVQIAPVQQ KGLETQLASL SDVLGEFFQV RDDYKNLTEE
YTGQKGFCED LDECKFSYPL IHALTSQPKN VQLRGILQQS RSAGGLDVPL KETVLSHLRQ
AGSIEYTEAK MGELMEKITD SVVSLEGETG SPNWVVRLLI HRLKV
