5EAS2_NICAT
ID 5EAS2_NICAT Reviewed; 548 AA.
AC Q84LF0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=5-epi-aristolochene synthase 2;
DE Short=NaEAS37;
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, INDUCTION BY
RP HERBIVORY, AND TISSUE 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 -!- INDUCTION: Up-regulated in shoots upon feeding by insect larvae.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF484125; AAP05762.1; -; mRNA.
DR AlphaFoldDB; Q84LF0; -.
DR SMR; Q84LF0; -.
DR BioCyc; MetaCyc:EAS37-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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 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 2"
FT /id="PRO_0000412245"
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; 63190 MW; 93B676A7FA7FBB88 CRC64;
MASAAVANYE EEIVRPVADF SPSLWGDQFL SFSIDNQIAE KYAQEIEALK EQTRSMLLAT
ARKLADTLNL IDTIERLGIA YHFEKEIDEI LDQIYNQNST FDDLCTSALQ FRLLRQHGFN
ISPQIFSKFQ DENGKFKESL ASDVLGLLNL YEASHVRTHT DNILEDALAF STVHLESAAP
YMNSPLREQV THALEQCLHK GVPRVETRFF ISSIYEKEES KNDMLLRFAK LDFNLLQMLH
KQELAEVSRW WKDLNFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVML VKTISMISIV
DDTFDAYGTV KELEAYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE KELSSAGRSH
IVCHAIERMK EVVRNYNVES TWFIEGYKPP VSEYLSNALA TTTYYYLATT SYLGMKSVAE
QDFEWLSKNP KILEASVIIC RVIDDTATYE VEKSRGQIAT GIECCMRDYG VSTKEAMDKF
QKMAETAWKD LNEGLLRPTP ISAEFLTPIL NLARIVEVTY IHNLDGYTHP EKVLKPHIID
LLVESIQI
