CAS_ABIBA
ID CAS_ABIBA Reviewed; 867 AA.
AC H8ZM73;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Bifunctional cis-abienol synthase, chloroplastic;
DE EC=4.2.1.133;
DE EC=4.2.3.140;
DE AltName: Full=Diterpene synthase TPS4;
DE Short=AbdiTPS4;
DE Flags: Precursor;
GN Name=CAS;
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, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP 403-ASP--ASP-405 AND ASP-622, AND 3D-STRUCTURE MODELING.
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 the biosynthesis of cis-abienol, a labdane
CC diterpene that can be used as synthesis precursor of ambergris
CC substitution fragance products. Bifunctional class I/II enzyme in which
CC both the bicyclization and water capture occur in the class II active
CC site, resulting in an intermediary labda-13-en-8-ol diphosphate, which
CC undergoes cleavage of the diphosphate group and final deprotonation at
CC the class I active site. No activity with copalyl diphosphate as
CC substrate. {ECO:0000269|PubMed:22337889}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-hydroxycopalyl diphosphate = cis-abienol + diphosphate;
CC Xref=Rhea:RHEA:34463, ChEBI:CHEBI:33019, ChEBI:CHEBI:64283,
CC ChEBI:CHEBI:68624; EC=4.2.3.140;
CC Evidence={ECO:0000269|PubMed:22337889};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = 8-
CC hydroxycopalyl diphosphate; Xref=Rhea:RHEA:32703, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:64283; EC=4.2.1.133;
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; JN254808; AEL99953.1; -; mRNA.
DR AlphaFoldDB; H8ZM73; -.
DR SMR; H8ZM73; -.
DR KEGG; ag:AEL99953; -.
DR BRENDA; 4.2.3.140; 13176.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102161; F:copal-8-ol 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; Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Plastid; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..867
FT /note="Bifunctional cis-abienol synthase, chloroplastic"
FT /id="PRO_0000423338"
FT MOTIF 403..406
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 622..626
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 403
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 622
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 622
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 763
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 767
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 771
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 403..405
FT /note="DID->AIA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22337889"
FT MUTAGEN 622
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22337889"
SQ SEQUENCE 867 AA; 99539 MW; 7C9A13BFDA8134C5 CRC64;
MALPVYSLKS HIPITTIASA KMNYTPNKGM ITANGRSRRI RLSPNKIVAC AGEADRTFPS
QSLEKTALFP DQFSEKNGTP SNFTPPNREF PPSFWNNDII NSITASHKVQ TGDRKRIQTL
ISEIKNVFNS MGDGETSPSA YDTAWVARIP AVDGSEQPQF PQTLEWILQN QLKDGSWGEE
FYFLAYDRLL ATLACIITLT IWRTGNVQLH KGIEFFRKQV VRMDDEADNH RPSGFEIVFP
AMLNEAKSLG LDLPYELPFI EQMVKKREAK LKMITTNVLY TIQTTLLYSL EGLHEIVDFD
KIIKLQSKDG SFLGSPASTA AVFMQTGNTK CLEFLEFVLR KFRNHVPSDY PLDLFERLWV
VDTVERLGID RHFKKEIKDA LDYVYSCWDE RGIGWAKDSP IADIDDTAMG LRILRLHGYN
VSPDVLKTFK DENGEFFCFM GQTQRGVTDM LNVYRCSQVA FPGETIMEEA KLCTERYLRN
ALENADAFDK WAIKKNIRGE VEYALKYPWH RSMPRLEVRS YIGNYGPNDV WLGKSLYMMP
YISNEKYLEL AKLDFNSVQS LHQEEIRELV RWCKSSGFTE LKFTRDRVVE TYFAVASSMF
EPEFSTCRAV YTKISVLLVI LDDLYDGYGS PDEIKLFSEA VKRWDLSLLE QMPDHMKICF
LGLYNTVNEV AEEGRKTQGH DVLGYIRNLW EIQLAAFTRE AEWSQGKYVP SFDEYIENAQ
VSIGVATILL ITILFTEEDD ILSHIDYGSK FLRLASLTAR LANDIKTYQE ERAHGEVVSA
IQCYMKDRPE ITEEEALKYV YGRMVNDLAE LNSEYLKSNE MPQNCKRLVF DTARVAQLFT
MEGDGLTYSD TMEIKEHIKK CLFEPAT
