EVAS_EMEVA
ID EVAS_EMEVA Reviewed; 716 AA.
AC A0A169T193;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Astellifadiene synthase {ECO:0000303|PubMed:27038368};
DE Short=SS {ECO:0000303|PubMed:27038368};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:27038368};
DE EC=4.2.3.- {ECO:0000269|PubMed:27038368};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:27038368};
DE Short=GGDP synthase {ECO:0000303|PubMed:27038368};
DE Short=GGS {ECO:0000303|PubMed:27038368};
DE EC=2.5.1.29 {ECO:0000269|PubMed:27038368};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase;
DE Short=GFDP synthase {ECO:0000303|PubMed:27038368};
DE EC=2.5.1.81 {ECO:0000269|PubMed:27038368};
GN Name=EvAS {ECO:0000303|PubMed:27038368};
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, DOMAIN, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX PubMed=27038368; DOI=10.1002/anie.201601448;
RA Matsuda Y., Mitsuhashi T., Lee S., Hoshino M., Mori T., Okada M., Zhang H.,
RA Hayashi F., Fujita M., Abe I.;
RT "Astellifadiene: structure determination by NMR spectroscopy and
RT crystalline sponge method, and elucidation of its biosynthesis.";
RL Angew. Chem. Int. Ed. 55:5785-5788(2016).
CC -!- FUNCTION: Bifunctional terpene synthase that converts DMAPP and IPP,
CC into astellifadiene (PubMed:27038368). The C-terminal prenyltransferase
CC (PT) domain of EvAS catalyzes formation of GFPP, whereas the N-terminal
CC terpene cyclase (TC) domain catalyzes the cyclization of GFPP to
CC astellifadiene (PubMed:27038368). {ECO:0000269|PubMed:27038368}.
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:27038368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:27038368};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81; Evidence={ECO:0000269|PubMed:27038368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:27038368};
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:27038368}.
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:27038368}.
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; LC113889; BAU98235.1; -; Genomic_DNA.
DR SMR; A0A169T193; -.
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.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Repeat; Transferase.
FT CHAIN 1..716
FT /note="Astellifadiene synthase"
FT /id="PRO_0000453640"
FT REGION 1..323
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:27038368"
FT REGION 324..713
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:27038368"
FT MOTIF 92..96
FT /note="DDXXD 1"
FT /evidence="ECO:0000305|PubMed:27038368"
FT MOTIF 223..231
FT /note="NSE/DTE"
FT /evidence="ECO:0000305|PubMed:27038368"
FT MOTIF 475..479
FT /note="DDXXD 2"
FT /evidence="ECO:0000305|PubMed:27038368"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 179..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 227..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 316..317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 436
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 439
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 468
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 484
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 485
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 562
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 563
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 598
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"
FT BINDING 625
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 716 AA; 82058 MW; 8C9F60B71FFF88C2 CRC64;
MEFKYSTLID PEMYETEGLC DGIPVRYHNN PELEEIDCLR CHEHWRENVG PLGVYKGGLA
DQWNGISIAI PEALPDRLGV VSYASEFAFV HDDVIDIAQH GNEQNDDLRV GFEQMIDAGA
IKYSTSGKRA LQSYIAKRML SIDRERAIIS LRAWLEFIEK TGRQEERRFN NEKEFLKYRI
YDVGMLFWYG LLTFAQKITI PENELTTCHE LAIPAYRHMA LLNDLVSWEK ERASSIALGK
DYCINFIFVA MEESGISEDE AKERCREEIK LATVDYLRVF DEAKDRIDLS HDTMLYLESL
LYSMSGNVVW GLQSPRYYTD AKFSQRQLDW IKNGLPLEVR LEDRVFGLSP SEDRVTHQAV
IENGLPESGL GKNGNSSNGV DVNKALLSAV LHEHLKGHAV FKMSDHEVKV KASNGRSLDT
KVLQAPYEYI TGLPSKRLRE QAIDAMNVWF RVPAEKLDLI KSITTILHNA SLMLDDVEDG
SELRRGNPST HTIFGLSQTI NSANYQLVRA LERVQKLEDS ESLLVFTEEL RNLYIGQSMD
LYWTGNLICP TMNEYFHMVE CKTGGLFRLF TRLMSLHSTS AVKVDPTTLS TRLGIYFQTR
DDYKNLVSTE YTKQKGYCED LEEGKFSLPL IHLIQAMPDN HVLRNILTQW RVTRKVTLAQ
KQVVLGLMEK SGSLKFTRET LASLYSGLEK SFTELEEKFG TENFQLKLIL QFLRTE
