5EAS3_NICAT
ID 5EAS3_NICAT Reviewed; 548 AA.
AC Q84LF2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=5-epi-aristolochene synthase 3;
DE Short=NaEAS12;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=12009313; DOI=10.1016/s0031-9422(02)00080-8;
RA Bohlmann J., Stauber E.J., Krock B., Oldham N.J., Gershenzon J.,
RA Baldwin I.T.;
RT "Gene expression of 5-epi-aristolochene synthase and formation of capsidiol
RT in roots of Nicotiana attenuata and N. sylvestris.";
RL Phytochemistry 60:109-116(2002).
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:12009313}.
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:12009313};
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 in roots, but not in shoots.
CC {ECO:0000269|PubMed:12009313}.
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; AF484123; AAP05760.1; -; mRNA.
DR RefSeq; XP_019264101.1; XM_019408556.1.
DR AlphaFoldDB; Q84LF2; -.
DR SMR; Q84LF2; -.
DR PRIDE; Q84LF2; -.
DR EnsemblPlants; OIT36657; OIT36657; A4A49_08386.
DR GeneID; 109241781; -.
DR Gramene; OIT36657; OIT36657; A4A49_08386.
DR KEGG; nau:109241781; -.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:EAS12-MON; -.
DR BRENDA; 4.2.3.61; 9729.
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 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Metal-binding; Plant defense.
FT CHAIN 1..548
FT /note="5-epi-aristolochene synthase 3"
FT /id="PRO_0000412246"
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; 63155 MW; DBDFDE9DA57A09D8 CRC64;
MASAAVGNYE EEIVRPVADF SPSLWGDQFL SFSIENQVAE KYAQEIEALK EQTRSMLLEN
GRKLADTLYL IDIIERLGIS YHFEKEIDDI LDQIYNQNSN CNDLCTSALQ FRLLRQHGFN
ISPEIFSKFQ DENGKFKESL ASDFLGLLNL YEASHVRTHA DDILEEALAF STIHLESAAP
HLKSPLREQV THALEQCLHK GVPRVETRFF ISSIYEKEQS KNDVLLRFAK LDFNLLQILH
KQELAEVSRW WKDLDFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVIL VKTISMISIV
DDTFDAYGTI KELETYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE KELSSAGRSH
IVCHAIERMK EVVKNYNVES TWFIEGYMPP VSEYLSNALA TTTYYYLATT SYLGMKSATE
QDFEWLSKNP KILEASVIIC RVIDDTATYE VEKSRGQIAT GIECCMRDYG VSTKEAMAKF
QGMAEAAWKD LNEGFLRPTP VSTEILFRIL NLARIVEVTY IHNLDGYTHP EKVLKPHINA
LLVDSIEI
