TPS1_MATCR
ID TPS1_MATCR Reviewed; 547 AA.
AC I6RAQ6;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=(-)-beta-caryophyllene synthase;
DE EC=4.2.3.57;
DE AltName: Full=Terpene synthase 1;
OS Matricaria chamomilla var. recutita (German chamomile) (Chamomilla
OS recutita).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Matricariinae; Matricaria.
OX NCBI_TaxID=127986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Bodegold;
RX PubMed=22682202; DOI=10.1186/1471-2229-12-84;
RA Irmisch S., Krause S.T., Kunert G., Gershenzon J., Degenhardt J.,
RA Koellner T.G.;
RT "The organ-specific expression of terpene synthase genes contributes to the
RT terpene hydrocarbon composition of chamomile essential oils.";
RL BMC Plant Biol. 12:84-84(2012).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of beta-
CC caryophyllene as the major product and trace amounts of alpha-humulene.
CC Produces exclusively the (-)-(E)-beta caryophyllene enantiomer.
CC {ECO:0000269|PubMed:22682202}.
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:22682202};
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 -!- TISSUE SPECIFICITY: High expression in disk florets, moderate
CC expression in ray florets and detected in leaves and stems, but not in
CC roots. {ECO:0000269|PubMed:22682202}.
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. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JQ255375; AFM43734.1; -; mRNA.
DR AlphaFoldDB; I6RAQ6; -.
DR SMR; I6RAQ6; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; 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; Manganese; Metal-binding.
FT CHAIN 1..547
FT /note="(-)-beta-caryophyllene synthase"
FT /id="PRO_0000421925"
FT MOTIF 300..304
FT /note="DDXXD motif"
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 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
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 547 AA; 63465 MW; A363669ACFFD8B84 CRC64;
MGKEEKVIRP IVHFSPSVWA DQFHIFRDEQ AEQANVEQVV NEMRKDVRKD IMSSLDVQAE
HTNLLKLIDA IQRLGIAYHF EEEIEQALKH IYDTYGDDWK GRSPSLWFRI LRQQGYYVSC
DILKNYKEED GSFKESLANN VEGLLELYEA TYLGVQGEDI LDDALVFTRT CLEKIAKDLV
HSNPTLSTHI QEALKQPLHK RLTRLEALCY IPMYEQLASH NESLLKLAKL DFNLLQSLHR
KELSEVSRWW KGLDVPNNLP YARDRMVECY FWALGVYFEP KYSRARIFLA KVISLATVLD
DTYDAYGIYE ELKIFTEAIQ GWSITCMHTL PEYMKLLYEG VLNIYKEMEE IIGSEGKAHH
LSYAKESMKE FIRSYMMEAK WANEGYVPTA EEHMAVAFVS SGYSMLATTC FVGMGDIVTD
EAFEWSLTKP PIIKASCAIA RLMDDIHSQK DEKERIHVAS SVESYMKQYD VTEEHVHKVF
HQKIEDAWKD ITRESLVCKD IPMPLMMRVI NLARVMDVLY THKDGFTNVG EELQDHIKSL
LVHPIPI
