STLSS_EMEVA
ID STLSS_EMEVA Reviewed; 714 AA.
AC A0A0P0ZEM1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Stellatatriene synthase {ECO:0000303|PubMed:26351860};
DE Short=SS {ECO:0000303|PubMed:26351860};
DE AltName: Full=Stellatic acid biosynthetis gene clusters protein Stl-SS {ECO:0000303|PubMed:26351860};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:26351860};
DE Short=GGDP synthase {ECO:0000303|PubMed:26351860};
DE Short=GGS {ECO:0000303|PubMed:26351860};
DE EC=2.5.1.- {ECO:0000269|PubMed:26351860};
DE Includes:
DE RecName: Full=stellata-2,6,19-trien synthase {ECO:0000303|PubMed:26351860};
DE EC=4.2.3.178 {ECO:0000269|PubMed:26351860};
GN Name=Stl-SS {ECO:0000303|PubMed:26351860};
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], DOMAIN, FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX PubMed=26351860; DOI=10.1021/acs.orglett.5b02404;
RA Matsuda Y., Mitsuhashi T., Quan Z., Abe I.;
RT "Molecular basis for stellatic acid biosynthesis: a genome mining approach
RT for discovery of sesterterpene synthases.";
RL Org. Lett. 17:4644-4647(2015).
CC -!- FUNCTION: Multifunctional diterpene synthase; part of the gene cluster
CC that mediates the biosynthesis of the sesterterpene stellatic acid
CC (PubMed:26351860). The first step in the pathway is performed by the
CC stellatatriene synthase that possesses both prenyl transferase and
CC terpene cyclase activity, converting isopentenyl diphosphate and
CC dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and
CC then converting GGDP into stellata-2,6,19-triene (PubMed:26351860). The
CC cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive
CC oxidation reactions on the C-20 methyl group to generate the carboxylic
CC acid of stellatic acid (PubMed:26351860).
CC {ECO:0000269|PubMed:26351860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + 4 isopentenyl diphosphate =
CC (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate;
CC Xref=Rhea:RHEA:66860, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:128769;
CC Evidence={ECO:0000269|PubMed:26351860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66861;
CC Evidence={ECO:0000269|PubMed:26351860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E,14E)-geranylfarnesyl diphosphate = diphosphate +
CC stellata-2,6,19-triene; Xref=Rhea:RHEA:54076, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:138048; EC=4.2.3.178;
CC Evidence={ECO:0000269|PubMed:26351860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54077;
CC Evidence={ECO:0000269|PubMed:26351860};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:26351860}.
CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}.
CC -!- DOMAIN: The characteristic DDXXD motif for binding a trinuclear Mg(2+)
CC cluster is conserved in both the N-terminal terpene cyclase and C-
CC terminal prenyl transferase domains. {ECO:0000305|PubMed:26351860}.
CC -!- DOMAIN: The Mg(2+)-binding NSE motif in the terpene cyclase domain is
CC not completely conserved, since the asparagine residue in the is
CC substituted with histidine. {ECO:0000305|PubMed:26351860}.
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; LC073704; BAT32889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0ZEM1; -.
DR SMR; A0A0P0ZEM1; -.
DR KEGG; ag:BAT32889; -.
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..714
FT /note="Stellatatriene synthase"
FT /id="PRO_0000452514"
FT REGION 1..325
FT /note="stellata-2,6,19-trien synthase"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 326..713
FT /note="Geranylgeranyl diphosphate synthase"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 332..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 92..96
FT /note="DDXXD motif 1"
FT /evidence="ECO:0000305|PubMed:26351860"
FT MOTIF 276..284
FT /note="NSE motif"
FT /evidence="ECO:0000305|PubMed:26351860"
FT MOTIF 473..477
FT /note="DDXXD motif 2"
FT /evidence="ECO:0000305|PubMed:26351860"
FT COMPBIAS 338..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 179..182
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 434
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 437
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 466
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 482
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 483
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 560
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 561
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 603
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 613
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 623
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 632..633
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ SEQUENCE 714 AA; 80706 MW; DA520A976523611F CRC64;
MEYKFSTVVD PGTYETHGLC EGYEVRYHKN AELEDIGCLR CQEHWRQSVG PLGAFKGTLG
NPFNLLSLVI PECLPDRLSI VGFANELAFI HDDVTDIVQY GDAHNNDFKE AFNSMATTGS
MENAASGKRA LQAYIAREMV RIDKERAIPT IKAWAKFVDY GGRQETTRFT SEKEYTEYRI
QDIGLWFWYG LLSFAMALDV PEHEREMCHE VCRTAYVQIM LVHDLASWEK EKLNAAALGK
DVITNIIFVL MEEHGISEEE AKERCRETAK TLAADYLKIV EEYKARDDIS LDSRKYIESW
LYTISGNTVW SFICPRYNSS GSFSDHQLEL MKNGVPKDPA SGSTNGTSNG TSNGTSHVAV
NGNGHVTNDD LSANGIKTDG ELLSAITMEH LKNRNSFKLG DHDQEVKSLH GHGQALDPRV
LQAPYEYITA LPSKGLREQA IDALNVWFRV PTAKLEIIKS ITTILHNASL MLDDVEDGSE
LRRGKPATHN IFGLGQTINS ANYQLVRALQ ELQKLGDARS LLVFTEELHN LYVGQSMDLY
WTSNLVCPSM HEYFQMIEHK TGGLFRLFGR LMAVHSTNPV QVDLTDFTNH LGRYFQTRDD
YQNLVSAEYT KQKGFCEDFE EGKFSLPMIH LMQTMPDNLV LRNVWTQRRV NGTATHGQKQ
TILNLMKEAG TLKFTQDSLG VLYSDVEKSV AELESKFGIE NFQLRLIMEL LKTG
