ID   5EAS4_NICAT             Reviewed;         548 AA.
AC   Q84LG0;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable 5-epi-aristolochene synthase 4;
DE            EC=4.2.3.61;
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hui D., Li H.;
RT   "Microarray analysis of insect-induced changes in transcript
RT   accumulation.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cyclization of trans,trans-farnesyl diphosphate
CC       (FPP) to the bicyclic intermediate 5-epi-aristolochene, initial step in
CC       the conversion of FPP to the sesquiterpenoid antifungal phytoalexin
CC       capsidiol. Produces germacrene A as an enzyme-bound intermediate that
CC       is not released by the enzyme, but is further cyclized to produce the
CC       bicyclic 5-epi-aristolochene (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (+)-5-epi-aristolochene +
CC         diphosphate; Xref=Rhea:RHEA:28635, ChEBI:CHEBI:23925,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.61;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AF542544; AAO85555.1; -; mRNA.
DR   AlphaFoldDB; Q84LG0; -.
DR   SMR; Q84LG0; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102698; F:5-epi-aristolochene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Magnesium; Metal-binding; Plant defense.
FT   CHAIN           1..548
FT                   /note="Probable 5-epi-aristolochene synthase 4"
FT                   /id="PRO_0000412247"
FT   MOTIF           301..305
FT                   /note="DDXXD motif"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  62897 MW;  F822E84CA1BF2BB8 CRC64;
     MASAAVGNYE EEIVRPVADF SPSLWGDHFL SFSIDNHVAQ KYAQEIEPLK EQTRSMLVAT
     GRKLVDTLNL IDTIERLGIS YHFEKEIDEI LDQIYNQNSN SSDLFTSALL FRLLRQHGFN
     ISPEIFSKFQ DENGKFKESL ASDVVGLLNL YEASHVRTHA DDILEAALAF STIHLESAAP
     HLKSPLREQV AHALEQCLHK GVPRVETRFF ISSIYEKEQS KNNVLLRFAI LDFNLLQMLH
     KQELAEVSRW WKDLDFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVML VKTISMISIV
     DDTFDAYGTV KELETYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE KELSSAGRSH
     IVCHAIERMK EVVRNYNVES TWFIEGYMPP VSEYLSNALA TTTYYYLATT SYLGMKSATE
     QDFEWLSKNP KILEASVIIC RVIDDTATYE VEKSRGQIAT GIECCMRDYG VSTKEAMDKF
     QQMAETAWKD LNEGLLRPTP VSAELLTPIL NLARIVEVTY IHNLDGYTHP EKVLKPHIIG
     LLVDSIDI