MPIM1_PINBN
ID MPIM1_PINBN Reviewed; 868 AA.
AC M4HY08;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Monofunctional pimaradiene synthase {ECO:0000303|PubMed:23370714};
DE Short=PbmPIM1 {ECO:0000303|PubMed:23370714};
DE EC=4.2.3.147 {ECO:0000269|PubMed:23370714};
GN Name=TPS-mPim1 {ECO:0000303|PubMed:23370714};
OS Pinus banksiana (Jack pine) (Pinus divaricata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3353;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=23370714; DOI=10.1104/pp.112.208546;
RA Hall D.E., Zerbe P., Jancsik S., Quesada A.L., Dullat H., Madilao L.L.,
RA Yuen M., Bohlmann J.;
RT "Evolution of conifer diterpene synthases: diterpene resin acid
RT biosynthesis in lodgepole pine and jack pine involves monofunctional and
RT bifunctional diterpene synthases.";
RL Plant Physiol. 161:600-616(2013).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury. Involved in diterpene (C20)
CC olefins biosynthesis. Monofunctional enzyme lacking the DXDD motif in
CC the class II active site relevant for the cyclization of geranylgeranyl
CC diphosphate (GGPP). Requires (+)-copalyl diphosphate ((+)-CPP) as
CC substrate, but no activity with GGPP or ent-CPP. Pimaradiene is the
CC major products of the enzyme. {ECO:0000269|PubMed:23370714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + pimara-8(14),15-diene;
CC Xref=Rhea:RHEA:42984, ChEBI:CHEBI:8210, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.147;
CC Evidence={ECO:0000269|PubMed:23370714};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000305}.
CC -!- MISCELLANEOUS: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif important
CC for the catalytic activity in the class I active site is degenetated,
CC but the Mg(2+) binding sites are conserved. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; JQ240315; AFU73867.1; -; mRNA.
DR AlphaFoldDB; M4HY08; -.
DR SMR; M4HY08; -.
DR KEGG; ag:AFU73867; -.
DR BRENDA; 4.2.3.147; 4842.
DR UniPathway; UPA00924; -.
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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Plant defense.
FT CHAIN 1..868
FT /note="Monofunctional pimaradiene synthase"
FT /id="PRO_0000431414"
FT BINDING 620
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 620
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 764
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 768
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 868 AA; 100159 MW; D294869391CCE8AC CRC64;
MAMPLCSLTS YNPITTTLRG HHFLTINAYV KTQCIPCFFI KLHTRSSASK QRIIDLRSGS
SNIVACVGEG ATSLSSHSDI MKTGKREEIP PGVWKDDISD SIMSSHKPEA DEKRVEILIA
EIKSMFRGMG DGETTPSAYD TAWVAKIPAL DGSDHPHFPQ TLQWILQNQL QDGSWGEGTY
FSAYDRLLAT LACIITLTVW RTGQTQVRQG IEFFRKHAGT MEDEADNHQP IGFEFVFPAM
INEAKSLCLD LPYDTPFIKQ IIEKREAKLK MIPTDTLYTV PTTFLHYLEG LQEIIDCQKI
IKLQSKDGSF LSSPASTAAV FMCTGNTKCL EFLNFVLIKF GNHVPCQYPL DLFERLWAVD
IVERLGIDRH FKKEIKDALD YVYSHWDERG IGWARENPVA YIDVMATGIR ILRLHRYNVS
SDILKTFRDE NGEFYRFPGQ SERGVTDMLN LNRCSHVAFP GETVMEEAKL CTERYLWNAL
ENVNPLDKWD LKENIRGEVE YALKYPWLRR LPRLETRNYI EHYGANDVWL GKMMHMMPYI
NDRKYLELAK LDFNNVQSIH QKELRELRRW WKSSGFAELN FLPDRVAEIF FSIASSMFEP
ELATCRAVYT KSTLCTVILD GFYDVHGSAE DIMLFNEAVK RWDHSLLDRM PEHIKTCFLA
LYNVVNEIAE EGRKRQGHDV LPYIRNLWEI QLESFTKEAE WSRAEHVPSF HEYIEAAAIS
SALPTLVLIG VIFTGEVLTD HILSQIDYRS KFAYLMSLTG RLANDTKTYQ VERSRGEVAS
AIQCYMKENP ELSEEEALEY IYRLMENALA DFKREFLKTK DVPEYCRRLV FDNARSMQLI
YMEGDGFKLS HETEIKEHVK KILFEPVA
