QH6_ARTAN
ID QH6_ARTAN Reviewed; 582 AA.
AC Q94G53;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=(-)-beta-pinene synthase, chloroplastic;
DE EC=4.2.3.120;
DE Flags: Precursor;
GN Name=QH6;
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, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=12226526; DOI=10.1104/pp.006544;
RA Lu S., Xu R., Jia J.W., Pang J., Matsuda S.P., Chen X.Y.;
RT "Cloning and functional characterization of a beta-pinene synthase from
RT Artemisia annua that shows a circadian pattern of expression.";
RL Plant Physiol. 130:477-486(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hui Y.-Y., Yang H.-Y., Sun T.-H., Wu Y.;
RT "HY5 confers the circadian expression of monoterpene synthase gene qh6.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Monoterpene synthase converting geranyl diphosphate to (-)-
CC beta-pinene and (-)-alpha-pinene in a 94:6 ratio.
CC {ECO:0000269|PubMed:12226526}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate;
CC Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.120;
CC Evidence={ECO:0000269|PubMed:12226526};
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young leaves. Detected in mature
CC leaves, inflorescences and stems, but not in roots.
CC {ECO:0000269|PubMed:12226526}.
CC -!- INDUCTION: Circadian-regulation. Expression peaked after 9 hours in
CC light. Down-regulated by wounding and elicitor treatment.
CC {ECO:0000269|PubMed:12226526}.
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. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AF276072; AAK58723.1; -; mRNA.
DR EMBL; GU929215; ADR64206.1; -; Genomic_DNA.
DR AlphaFoldDB; Q94G53; -.
DR SMR; Q94G53; -.
DR KEGG; ag:AAK58723; -.
DR BRENDA; 4.2.3.119; 7150.
DR BRENDA; 4.2.3.120; 7150.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..87
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 88..582
FT /note="(-)-beta-pinene synthase, chloroplastic"
FT /id="PRO_0000418829"
FT MOTIF 337..341
FT /note="DDXXD motif"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 582 AA; 67507 MW; 19775F7793269933 CRC64;
MASMCTFSSP FLLCNSSISR TNIVACNKQT STLQAQVKNV ATIETTNRRS ANYAPSLWSY
DFVQSLSSKY KGDNYMARSR ALKGVVRTMI LEANGIENPL SLLNLVDDLQ RLGISYHFLD
EISNVLEKIY LNFYKSPEKW TNMDLNLRSL GFRLLRQHGY HIPQEIFKDF IDVNGNFKGD
IISMLNLYEA SYHSVEEESI LDDAREFTTK YLKETLENIE DQNIALFISH ALVFPLHWMV
PRVETSWFIE VYPKKVGMNP TVLEFAKLDF NILQAVHQED MKKASRWWKE TCWEKFGFAR
DRLVENFMWT VAENYLPHFQ TGRGVLTKVN AMITTIDDVY DVYGTLPELE LFTNIVNSWD
INAIDELPDY LKICFLACYN ATNELSYNTL TNKGFFVHPY LKKAWQDLCN SYIIEAKWFN
DGYTPTFNEF IENAYMSIGI APIIRHAYLL TLTSVTEEAL QHIERAESMI RNACLIVRLT
NDMGTSSDEL ERGDIPKSIQ CYMHESGATE MEARAYIKQF IVETWKKLNK ERQEIGSEFP
QEFVDCVINL PRMGHFMYTD GDKHGKPDMF KPYVFSLFVN PI
