5EAS_CAPAN
ID 5EAS_CAPAN Reviewed; 559 AA.
AC O65323;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=5-epiaristolochene synthase;
DE EC=4.2.3.61;
GN Name=EAS; Synonyms=PEAS;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY UV
RP TREATMENT, AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=9816674; DOI=10.1093/oxfordjournals.pcp.a029452;
RA Back K., He S., Kim K.U., Shin D.H.;
RT "Cloning and bacterial expression of sesquiterpene cyclase, a key branch
RT point enzyme for the synthesis of sesquiterpenoid phytoalexin capsidiol in
RT UV-challenged leaves of Capsicum annuum.";
RL Plant Cell Physiol. 39:899-904(1998).
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. {ECO:0000269|PubMed:9816674}.
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 Evidence={ECO:0000269|PubMed:9816674};
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 -!- TISSUE SPECIFICITY: Expressed only in treated leaves an not detected in
CC control leaves. {ECO:0000269|PubMed:9816674}.
CC -!- INDUCTION: Up-regulated by UV treatment. {ECO:0000269|PubMed:9816674}.
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; AF061285; AAC61260.1; -; mRNA.
DR PIR; T08174; T08174.
DR AlphaFoldDB; O65323; -.
DR SMR; O65323; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000189700; Genome assembly.
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 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Metal-binding; Plant defense.
FT CHAIN 1..559
FT /note="5-epiaristolochene synthase"
FT /id="PRO_0000412243"
FT MOTIF 312..316
FT /note="DDXXD motif"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 559 AA; 65098 MW; DB7F07B3E3A26DC0 CRC64;
MASVAVENNV VNHIAEEIIR PVADFSPSLW GDRFLSFSID NQVETKYAQE IEPLKEQTRS
MLLASGRKLS ETLNLIDVIE RLGIAYHFEK EIDEILDRIY NENSNFEGDV YNEDLCTCRL
QFRLLRQHGY NISLKIFSKF LDGNGRLKES LASDVLGLLS LYEASHVRSH GEDILEDALA
FSTTHLESAT PHLEYPLKEQ VRHALEQSLH KGIPRIEIQF FISSVYDKQA IKNDVLLRFA
KLDYNMLQML HKQELAEVSR WWKDLNFVNT LPYARDRVVE CYFWALGVYY EPQYSQARVM
LVKTIAMISI VDDTYDAYGT VDELAIYTDV IQRWDIKEID SLPDYMKISY KALLDLYKDY
EKEMSRDGRS HVVYYAKERL KELVKSYNIE AKWFIEGHMP PASEYLRNAF VTTTYYYLAT
TSYLGMKYAK EQQFEWLSKN PKILEGCVTI CRVIDDIATY EVEKNRGQLS TGIECYMRDY
SVSTKEAMAK FQEMGESGWK DINEGMLRPT PIPMEFLSRI LNLARLVDVT YKHNEDGYTH
PEKVIKPHII AMVVDSFKI
