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MPIM1_PINCO
ID   MPIM1_PINCO             Reviewed;         868 AA.
AC   M4HYC8;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Monofunctional pimaradiene synthase {ECO:0000303|PubMed:23370714};
DE            Short=PcmPIM1 {ECO:0000303|PubMed:23370714};
DE            EC=4.2.3.147 {ECO:0000269|PubMed:23370714};
GN   Name=TPS-mPim1 {ECO:0000303|PubMed:23370714};
OS   Pinus contorta (Shore pine) (Lodgepole pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3339;
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; JQ240316; AFU73868.1; -; mRNA.
DR   AlphaFoldDB; M4HYC8; -.
DR   SMR; M4HYC8; -.
DR   KEGG; ag:AFU73868; -.
DR   BRENDA; 4.2.3.147; 4843.
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_0000431415"
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;  100104 MW;  D1A07A6856DFC633 CRC64;
     MAMPLCSLTS YNPITTTLRG HHFLTINAYV KTQCIPCFFI KLHTRSSGSK QRIIDLRSGS
     SNIVACVGEG ATSLSSHSDI MKTAKREEIP PGVWKDDISD SIMSSHKPEA DEKRVEILIA
     EIKSMFRGMG DGETTPSAYD TAWVAKIPAL DGSDHPHFPQ TLQWILQNQL QDGSWGEGTY
     FSTYDRLLAT LACIITLTVW RTGQTQVRQG IEFFRKHAGT MEDEADNHQP IGFEFVFPAM
     INEAKSLCLD LPYDTPFIKQ IIEKREAKLK MIPTDTLYTV PTTFLYYLEG LQEIIDCQKI
     IKLQSKDGSF LSSPASTAAV FMCTGNTKCL EFLNFVLIKF GNHVPCQYPL DLFERLWAVD
     IVERLGIDRH FKKEIKDALD YVYSHWDERG IRWARENPVA YIDVMATGIR ILRLHRYNVS
     SDILKTFRDE NGEFYRFPGQ SERGVTDMLN LNRCSHVAFP GETVMEEAKL CTERYLWNAL
     ENVNPLDKWG LKENIRGEVE YALKYPWLRR LPRLETRNYI EHYGANDVWL GKMMHMMPYI
     NDRKYLELAK LDFNNVQSIH QKELRELRRW WKSSGFAELN FLPDRVAEIF FSIASSMFEP
     ELATCRAVYT KSTLCTVILD GFYDVHGSAE DIMLFNEAVK RWDHSLLDRM AEHIKTCFLA
     LYNVVNEIAE EGRKRQGHDV LPYIRNLWEI QLESFTKEAE WSRAEHVPSF HEYIEAAAIS
     SALPTLVLIG VIFTGEVLTD HILSQIDYRS KFAYLMSLTG RLANDTKTYQ VERGQGEVAS
     AIQCYMKENP ELSEEEALEY IYRLMENALA DFKCEFLNTK DVPEYCRRLV FDNARSMQLI
     YMEGDGFKLS HETEIKQHVK KILFEPVA
 
 
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