MISO1_PINBN
ID MISO1_PINBN Reviewed; 876 AA.
AC M4HXW5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Monofunctional isopimaradiene synthase, chloroplastic {ECO:0000303|PubMed:23370714};
DE Short=PbmIso1 {ECO:0000303|PubMed:23370714};
DE EC=4.2.3.44 {ECO:0000269|PubMed:23370714};
DE Flags: Precursor;
GN Name=TPS-mISO1 {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 {ECO:0000312|EMBL:AFU73865.1};
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. Isopimaradiene is the
CC major products of the enzyme followed by sandaracopimaradiene.
CC {ECO:0000269|PubMed:23370714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + isopimara-7,15-diene;
CC Xref=Rhea:RHEA:26128, ChEBI:CHEBI:33019, ChEBI:CHEBI:52280,
CC ChEBI:CHEBI:58635; EC=4.2.3.44;
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity in the class I active site, presumably through
CC binding to Mg(2+). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; JQ240313; AFU73865.1; -; mRNA.
DR AlphaFoldDB; M4HXW5; -.
DR SMR; M4HXW5; -.
DR BRENDA; 4.2.3.B25; 4842.
DR UniPathway; UPA00924; -.
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: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 Chloroplast; Lyase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..876
FT /note="Monofunctional isopimaradiene synthase,
FT chloroplastic"
FT /id="PRO_0000431412"
FT MOTIF 628..632
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 632
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 632
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
FT BINDING 776
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 780
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 876 AA; 100632 MW; 1CF943A255463491 CRC64;
MAMPSYSSLS SHISITTTHT RPHPIFPCYY DTQSIPRFFI SSDTGSSASK QRNIYLRLGS
RKIIAGVGEG ATSLSSHSDK MKTDSFPDPK LAKRDFPPGF WKDDIIDSIM SSNKVAAADE
ERVETLISEI KSMFRGMGDG ETTPSAYDTA WVAKIPALDG SDHPHFPQTL QWILLNQLKD
GSWGEEHHFL TYDRLLATLA CIITLTVWRT GKTQVQKGIE FFKKHAGMME DEADHRQPSG
FEFVFPAMIN EAKSLCLDLP YELPFIKQII KKREAKLKRI PTDLLYTVPT IFLYYLEGLQ
EIVEWHKIIK LQSKDGSFLS SPASTAAVFM STGNTKCLEF LNFVLMKFGN HAPCHYPIDL
LERLWAVDTV QRLGIDRYFK EEIKEALDYI YSHWGERGIG WARENPVADI GVTAMGLRIL
RLNGYNVSSD VLRTFRDENG EFFSFMGQTE RGVIDMLNLN RCSHVAFPGE TVMEEAKHCT
ERYLWNALED VDALDKWGLK KNIRGEVEYA LKYPWLRSLP RLEARSYIEN YGPNDAWLGK
TMYIMPYINN GKYLELAKLD FNNVQSIHQK ELRELRRWWK SSGFAELNFT RDRVAEIFFS
IASSMFEPEL ATCRAVYTKS TICTVILDDL YDAHGSVEDI KLFNEAVKRW DLFLLDRMPE
HIKICFLGLY NLVNEIAEEG RKRQGRDVLG YIRNLWEIQL ETFMKEAEWS EAKYVPSFHE
YIETASVSIA GATLVLFGVL FTGEVLTDHI LSQIDYRSKF AYLMGLTGRL INDTKTYQAE
RGEGEVASAI QCYMKDHPEF SEEEALKQIY TLMENALADL KEEFLKAKDV PDKCKRLVFD
YARSMQLFYQ QGDGFTLAPN MEIKQHVKKI LFEPVP
