ID   AZIS_OCIBA              Reviewed;         541 AA.
AC   Q5SBP4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Alpha-zingiberene synthase;
DE            EC=4.2.3.65;
GN   Name=ZIS;
OS   Ocimum basilicum (Sweet basil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC   Ocimum.
OX   NCBI_TaxID=39350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15516500; DOI=10.1104/pp.104.051318;
RA   Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E.,
RA   Lewinsohn E., Pichersky E.;
RT   "The biochemical and molecular basis for the divergent patterns in the
RT   biosynthesis of terpenes and phenylpropenes in the peltate glands of three
RT   cultivars of basil.";
RL   Plant Physiol. 136:3724-3736(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=18643974; DOI=10.1111/j.1365-313x.2008.03599.x;
RA   Davidovich-Rikanati R., Lewinsohn E., Bar E., Iijima Y., Pichersky E.,
RA   Sitrit Y.;
RT   "Overexpression of the lemon basil alpha-zingiberene synthase gene
RT   increases both mono- and sesquiterpene contents in tomato fruit.";
RL   Plant J. 56:228-238(2008).
CC   -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of alpha-
CC       zingiberene and other sesquiterpenes from trans,trans-farnesyl
CC       diphosphate (FPP). May have an additional monoterpene synthase
CC       activity. {ECO:0000269|PubMed:15516500, ECO:0000269|PubMed:18643974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = alpha-zingiberene +
CC         diphosphate; Xref=Rhea:RHEA:28643, ChEBI:CHEBI:10115,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.65;
CC         Evidence={ECO:0000269|PubMed:15516500};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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   -!- 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; AY693646; AAV63788.1; -; mRNA.
DR   AlphaFoldDB; Q5SBP4; -.
DR   SMR; Q5SBP4; -.
DR   KEGG; ag:AAV63788; -.
DR   BRENDA; 4.2.3.65; 4385.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0102884; F:alpha-zingiberene 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: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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..541
FT                   /note="Alpha-zingiberene synthase"
FT                   /id="PRO_0000399252"
FT   MOTIF           296..300
FT                   /note="DDXXD motif"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         441
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  62858 MW;  FBE67A5DE1732320 CRC64;
     MESRRSANYQ ASIWDDNFIQ SLASPYAGEK YAEKAEKLKT EVKTMIDQTR DELKQLELID
     NLQRLGICHH FQDLTKKILQ KIYGEERNGD HQHYKEKGLH FTALRFRILR QDGYHVPQDV
     FSSFMNKAGD FEESLSKDTK GLVSLYEASY LSMEGETILD MAKDFSSHHL HKMVEDATDK
     RVANQIIHSL EMPLHRRVQK LEAIWFIQFY ECGSDANPTL VELAKLDFNM VQATYQEELK
     RLSRWYEETG LQEKLSFARH RLAEAFLWSM GIIPEGHFGY GRMHLMKIGA YITLLDDIYD
     VYGTLEELQV LTEIIERWDI NLLDQLPEYM QIFFLYMFNS TNELAYEILR DQGINVISNL
     KGLWVELSQC YFKEATWFHN GYTPTTEEYL NVACISASGP VILFSGYFTT TNPINKHELQ
     SLERHAHSLS MILRLADDLG TSSDEMKRGD VPKAIQCFMN DTGCCEEEAR QHVKRLIDAE
     WKKMNKDILM EKPFKNFCPT AMNLGRISMS FYEHGDGYGG PHSDTKKKMV SLFVQPMNIT
     I