ISO_ABIBA
ID ISO_ABIBA Reviewed; 852 AA.
AC H8ZM71;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Bifunctional isopimaradiene synthase, chloroplastic;
DE Short=AbIso;
DE AltName: Full=Diterpene synthase TPS2;
DE Short=AbdiTPS2;
DE Includes:
DE RecName: Full=Isopimara-7,15-diene synthase;
DE Short=Isopimaradiene synthase;
DE EC=4.2.3.44;
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12;
DE Flags: Precursor; Fragment;
GN Name=TPS-ISO;
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 (By similarity). Involved in
CC diterpene (C20) olefins biosynthesis. Bifunctional enzyme that
CC catalyzes two sequential cyclizations of geranylgeranyl diphosphate
CC (GGPP) to isopimara-7,15-diene. {ECO:0000250,
CC 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 = 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: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 -!- 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; JN254806; AEL99951.1; -; mRNA.
DR AlphaFoldDB; H8ZM71; -.
DR SMR; H8ZM71; -.
DR PRIDE; H8ZM71; -.
DR BRENDA; 4.2.3.B25; 13176.
DR BRENDA; 5.5.1.12; 13176.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050559; F:copalyl diphosphate 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..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..852
FT /note="Bifunctional isopimaradiene synthase, chloroplastic"
FT /id="PRO_0000423340"
FT MOTIF 385..388
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 604..608
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 604
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 604
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 608
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 608
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 756
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 852 AA; 98246 MW; 5212C5D2418AB871 CRC64;
HHLTANTQSI PHFSTTLNAG SSARKRRSLY LRWGKGSNKI IACVGEGATS VPYQSAEKND
SLYSSTLVKR EFPPGFWKDD LIDSLTSSHK VAASDEKRIE TLISEIKNMF RCMGYGETNP
SAYDTAWVAR IPALDGSDNP HFPETVEWIL QNQLKDGSWG EGFYFLAYDR ILATLACIIT
LTLWRTGETQ VHKGIEFFRT QAGKMEDEAD SHRPSGFEIV FPAMLKEAKI LGLDLPYDLP
FLKQIIEKRE AKLKRIPTDV LYALPTTLLY SLEGLQEIVD WQKIMKLQSK DGSFLSSPAS
TAAVFMRTGN KKCLDFLNFV LKKFGNHVPC HYPLDLFERL WAVDTVERLG IDRHFKEEIK
DALDYVYSHW DERGIGWARE NPVPDIDDTA MGLRILRLHG YNVSSDVLKT FRDENGEFFC
FLGQTQRGVT DMLNVNRCSH VSFPGETIME EAKLCTERYL RNALENVDAF DKWAFKKNIR
GEVEYALKYT WHKSMPRLEA RSYIENYGPN DAWLGKTVYR MPYISNEKYL ELAKLDFNKL
QSIHQTELQD LRRWWKSSGF SKLNFTRERV TEIYFSSASF MFEPEFSKCR EVYTKASIFT
LIFDDLYDAH GSLDDLKLFS EAVKRWDLSL LERMPQEMKI CFLGFYNTFN EIAEEVHKRQ
GRDMLGHIQN VWEILLAAYT KEAEWSKTKY VPSFDEYIEN ASVSITLGTI VLISTLFIGE
VLTDHVLSKI NHGSRFLHLM GLTGRLVNDT KTYQAERGQG EEASAIQCYM KDHPEISEEE
ALNHVYNVME NALQELNKEF VNNKEVPPNC RRLVFNTARI MQLFYMQGDG LTLSHDMEIK
DHVKTCLFIP IA
