TPSCM_MENPI
ID TPSCM_MENPI Reviewed; 551 AA.
AC Q5W283;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cis-muuroladiene synthase;
DE Short=MxpSS1;
DE EC=4.2.3.67;
OS Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC Mentha.
OX NCBI_TaxID=34256;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
RX PubMed=16083926; DOI=10.1016/j.phytochem.2005.06.012;
RA Prosser I.M., Adams R.J., Beale M.H., Hawkins N.D., Phillips A.L.,
RA Pickett J.A., Field L.M.;
RT "Cloning and functional characterisation of a cis-muuroladiene synthase
RT from black peppermint (Menthaxpiperita) and direct evidence for a chemotype
RT unable to synthesise farnesene.";
RL Phytochemistry 67:1564-1571(2006).
CC -!- FUNCTION: Involved in the formation of muuroladienes. Produces mainly
CC cis-muurola-3,5-diene and cis-muurola- 4(14),5-diene, but also smaller
CC amounts of gamma-cadinene and alpha-cadinene.
CC {ECO:0000269|PubMed:16083926}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = cis-muurola-3,5-diene +
CC diphosphate; Xref=Rhea:RHEA:29487, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61687, ChEBI:CHEBI:175763; EC=4.2.3.67;
CC Evidence={ECO:0000269|PubMed:16083926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = cis-muurola-4(14),5-diene +
CC diphosphate; Xref=Rhea:RHEA:29491, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61688, ChEBI:CHEBI:175763; EC=4.2.3.67;
CC Evidence={ECO:0000269|PubMed:16083926};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.91 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:16083926};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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}.
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DR EMBL; AJ786641; CAH10288.1; -; mRNA.
DR AlphaFoldDB; Q5W283; -.
DR SMR; Q5W283; -.
DR KEGG; ag:CAH10288; -.
DR BioCyc; MetaCyc:MON-14486; -.
DR BRENDA; 4.2.3.67; 3222.
DR SABIO-RK; Q5W283; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; 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: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; Manganese; Metal-binding; Plant defense.
FT CHAIN 1..551
FT /note="Cis-muuroladiene synthase"
FT /id="PRO_0000412248"
FT MOTIF 302..306
FT /note="DDXXD motif"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 551 AA; 63839 MW; 910E34C342DDAD57 CRC64;
MATNGVVISC LREVRPPMTK HAPSMWTDTF SNFSLDDKEQ QKRSETIEAL KQEARGMLMA
ATTPLQQMTL IDTLERLGLA FHFETEVEYK IEQINAAAED DGFDLFATAL RFRLLRQHQR
HVSCDVFDKF VDKDGKFEES LSNNVEGLLS LYEAAHVGFR EERILQEAVN FTRHHLEGAE
LDQSPLLIRE KVKRALEHPL HRDFPIVYAR LFISIYEKDD SRDELLLKLS KVNFKFMQNL
YKKELSQLSR WWNTWDLKSK LPYARDRVVE AYVWGVGYHY EPQYSYVRMG LAKGILIIGI
MDDTYDNYAT LNEAQLFTQV LDKWDRDEAD RLPEYMKIVY EFILSTCENY ERDAAKLGKS
FAAPYFKETV KQLARAFNQE QKWVMERQLP SFQDYVKNSE KTSCIYTMFA SIIPGLKSVT
QETIDWIKSE PTLATSTGMI GRYWDDIGSH LRESKGGEML TALDFHMKEY GLTKEEAASK
FEGLVEETWK DINKEFIATT NYNVGREIAI TFLNYARICE ASYSKTDGDA YLDPNVAKAN
VVALFVDAIV F
