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CARS_ARTAN
ID   CARS_ARTAN              Reviewed;         548 AA.
AC   Q8SA63;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Beta-caryophyllene synthase;
DE            EC=4.2.3.57;
GN   Name=QHS1;
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION BY WOUNDING AND ELICITORS.
RX   PubMed=12409018; DOI=10.1016/s0031-9422(02)00265-0;
RA   Cai Y., Jia J.W., Crock J., Lin Z.X., Chen X.Y., Croteau R.;
RT   "A cDNA clone for beta-caryophyllene synthase from Artemisia annua.";
RL   Phytochemistry 61:523-529(2002).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=21388533; DOI=10.1186/1471-2229-11-45;
RA   Olofsson L., Engstroem A., Lundgren A., Brodelius P.E.;
RT   "Relative expression of genes of terpene metabolism in different tissues of
RT   Artemisia annua L.";
RL   BMC Plant Biol. 11:45-45(2011).
CC   -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of beta-
CC       caryophyllene, a sesquiterpene with anti-inflammatory and anti-
CC       carcinogenic activities. Can use farnesyl diphosphate and (+)-
CC       chrysanthemyl diphosphate as substrates, but not geranylgeranyl
CC       diphosphate. Produces two irregular monoterpenes, yomogi alcohol and
CC       artemisia alcohol from (+)-chrysanthemyl diphosphate. Limited activity
CC       with geranyl diphosphate, leading to the production of limonene,
CC       terpinolene, beta-pinene, gamma-terpinene, alpha-terpinene and other
CC       minor products. {ECO:0000269|PubMed:12409018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC         diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC         Evidence={ECO:0000269|PubMed:12409018};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 uM for (2E,6E)-farnesyl diphosphate
CC         {ECO:0000269|PubMed:12409018};
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:12409018};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12409018}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in stem epidermis, cortex and
CC       stele. Detected in leaves, petioles and inflorescences, but not in
CC       roots. {ECO:0000269|PubMed:12409018, ECO:0000269|PubMed:21388533}.
CC   -!- DEVELOPMENTAL STAGE: Expression decreases with the age of the
CC       seedlings. {ECO:0000269|PubMed:12409018}.
CC   -!- INDUCTION: Up-regulated by wounding and by elicitor treatment.
CC       {ECO:0000269|PubMed:12409018}.
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. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF472361; AAL79181.1; -; mRNA.
DR   AlphaFoldDB; Q8SA63; -.
DR   SMR; Q8SA63; -.
DR   KEGG; ag:AAL79181; -.
DR   BioCyc; MetaCyc:MON-14912; -.
DR   BRENDA; 4.2.3.57; 7150.
DR   GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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; Manganese; Metal-binding.
FT   CHAIN           1..548
FT                   /note="Beta-caryophyllene synthase"
FT                   /id="PRO_0000412110"
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|UniProtKB:Q40577"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         445
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   548 AA;  63737 MW;  40B8E69751FF6654 CRC64;
     MSVKEEKVIR PIVHFPPSVW ADQFLIFDDK QAEQANVEQV VNELREDVRK DLVSSLDVQT
     EHTNLLKLID AIQRLGIAYH FEEEIEQALQ HIYDTYGDDW KGRSPSLWFR ILRQQGFYVS
     CDIFKNYKKE DGSFKESLTN DVEGLLELYE ATYLRVQGEG VLDDALVFTR TCLEKIAKDL
     VHTNPTLSTY IQEALKQPLH KRLTRLEALR YIPMYEQQAS HNESLLKLAK LGFNLLQSLH
     RKELSEVSRW WKGLDVPNNL PYARDRMVEC YFWALGVYFE PKYSQARIFL AKVISLATVL
     DDTYDAYGTY EELKIFTEAI QRWSITCIDM LPEYLKLLYQ GVLDIYIEME EIMGKEGKAH
     HLSYAKESMK EFIRSYMMEA KWANEGYVPT AEEHMSVAFV SSGYSMLATT CFVGMGDIVT
     DEAFKWALTK PPIIKASCAI ARLMDDIHSQ KEEKERIHVA SSVESYMKQY DVTEEHVLKV
     FNKKIEDAWK DITRESLVRK DIPMPLMMRV INLAQVMDVL YKHKDGFTNV GEELKDHIKS
     LLVHPIPI
 
 
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