LAS_ABIBA
ID LAS_ABIBA Reviewed; 844 AA.
AC H8ZM70;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Bifunctional abietadiene synthase, chloroplastic;
DE AltName: Full=Abietadiene cyclase;
DE AltName: Full=Diterpene synthase TPS1;
DE Short=AbdiTPS1;
DE AltName: Full=Levopimaradiene/abietadiene synthase;
DE Short=AbLAS;
DE Includes:
DE RecName: Full=Abietadiene synthase;
DE EC=4.2.3.18;
DE AltName: Full=Levopimaradiene synthase;
DE EC=4.2.3.32;
DE AltName: Full=Neoabietadiene synthase;
DE EC=4.2.3.132;
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12;
DE Flags: Precursor; Fragment;
GN Name=LAS;
OS Abies balsamea (Balsam fir) (Pinus balsamea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX NCBI_TaxID=90345;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22337889; DOI=10.1074/jbc.m111.317669;
RA Zerbe P., Chiang A., Yuen M., Hamberger B., Hamberger B., Draper J.A.,
RA Britton R., Bohlmann J.;
RT "Bifunctional cis-abienol synthase from Abies balsamea discovered by
RT transcriptome sequencing and its implications for diterpenoid fragrance
RT production.";
RL J. Biol. Chem. 287:12121-12131(2012).
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. Bifunctional enzyme that catalyzes two sequential
CC cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The
CC copalyl diphosphate (CPP) intermediate diffuses freely between the 2
CC active sites in the enzyme. {ECO:0000269|PubMed:22337889}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:58756; EC=5.5.1.12;
CC Evidence={ECO:0000269|PubMed:22337889};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate;
CC Xref=Rhea:RHEA:13873, ChEBI:CHEBI:30232, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.18;
CC Evidence={ECO:0000269|PubMed:22337889};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + neoabietadiene;
CC Xref=Rhea:RHEA:33987, ChEBI:CHEBI:29651, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.132;
CC Evidence={ECO:0000269|PubMed:22337889};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate;
CC Xref=Rhea:RHEA:25548, ChEBI:CHEBI:29616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.32;
CC Evidence={ECO:0000269|PubMed:22337889};
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.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity in the class II active site relevant for the cyclization of
CC GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the
CC 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; JN254805; AEL99950.1; -; mRNA.
DR AlphaFoldDB; H8ZM70; -.
DR SMR; H8ZM70; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050554; F:abietadiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0052678; F:levopimaradiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; 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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Plastid; Transit peptide.
FT TRANSIT <1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..844
FT /note="Bifunctional abietadiene synthase, chloroplastic"
FT /id="PRO_0000423339"
FT MOTIF 378..381
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 597..601
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 741
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 745
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT NON_TER 1
SQ SEQUENCE 844 AA; 97273 MW; 03CED90C8652E368 CRC64;
QSIPHFSTTL NAGSSARKRR SLYLRWGKGS NKIIACVGEG ATSVPYQSAE KNDSLYSSTL
VKREFPPGFW KDDLIDSLTS SHKVAASDEK RIETLISEIK NMFRCMGYGE TNPSAYDTAW
VARIPALDGS DNPHFPETVE WILQNQLKDG SWGEGFYFLA YDRILATLAC IITLTLWRTG
ETQVHKGIEF FRTQAGKMED EADSHRPSGF EIVFPAMLKE AKILGLDLPY DLPFLKQIIE
KREAKLKRIP TDVLYALPTT LLYSLEGLQE IVDWQKIMKL QSKDGSFLSS PASTAAVFMR
TGNKKCLDFL NFVLKKFGNH VPCHYPLDLF ERLWAVDTVE RLGIDRHFKE EIKEALDYVY
SHWDERGIGW ARENPVPDID DTAMGLRILR LHGYNVSSDV LKTFRDENGE FFCFLGQTQR
GVTDMLNVNR CSHVSFPGET IMEEAKLCTE RYLRNALENV DAFDKWAFKK NIRGEVEYAL
KYPWHKSMPR LEARSYIENY GPDDVWLGKT VYMMPYISNE KYLELAKLDF NKVQSIHQTE
LQDLRRWWKS SGFTDLNFTR ERVTEIYFSP ASFIFEPEFS KCREVYTKTS NFTVILDDLY
DAHGSLDDLK LFTESVKRWD LSLVDQMPQQ MKICFVGFYN TFNEIAKEGR ESQGRDVLGY
IQNVWKVQLE AYTKEAEWSE AKYVPSFNEY IENASVSIAL GTVVLISALF TGEVLTDEVL
SKIDRGSRFL QLMGLTGRLV NDTKTYQAER GQGEVASAIQ CYMKDHPKIS EEEALKHVYT
VMENSLEELN REFVNNKIPD IYRRLVFETA RIMQLFYMQG DGLTLSHDME IKEHVKNCLF
QPVA
