CABS_TOBAC
ID CABS_TOBAC Reviewed; 792 AA.
AC G3CCC1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cis-abienol synthase, chloroplastic {ECO:0000303|PubMed:22672125};
DE Short=NtABS {ECO:0000303|PubMed:22672125};
DE EC=4.2.3.140 {ECO:0000269|PubMed:22672125};
DE Flags: Precursor;
GN Name=ABS {ECO:0000303|PubMed:22672125};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=22672125; DOI=10.1111/j.1365-313x.2012.05068.x;
RA Sallaud C., Giacalone C., Toepfer R., Goepfert S., Bakaher N., Roesti S.,
RA Tissier A.;
RT "Characterization of two genes for the biosynthesis of the labdane
RT diterpene Z-abienol in tobacco (Nicotiana tabacum) glandular trichomes.";
RL Plant J. 72:1-17(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ambalema;
RX PubMed=23757397; DOI=10.1105/tpc.113.111013;
RA Matsuba Y., Nguyen T.T., Wiegert K., Falara V., Gonzales-Vigil E.,
RA Leong B., Schafer P., Kudrna D., Wing R.A., Bolger A.M., Usadel B.,
RA Tissier A., Fernie A.R., Barry C.S., Pichersky E.;
RT "Evolution of a complex locus for terpene biosynthesis in Solanum.";
RL Plant Cell 25:2022-2036(2013).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
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. {ECO:0000269|PubMed:22672125}.
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:22672125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:22672125}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in trichomes.
CC {ECO:0000269|PubMed:22672125}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The expression of both CPS2 and ABS is necessary and
CC sufficient to catalyze the biosynthesis of cis-abienol from
CC geranylgeranyl diphosphate in a heterologous system.
CC {ECO:0000305|PubMed:22672125}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HE588140; CCD33019.1; -; mRNA.
DR EMBL; KF000066; AGN95433.1; -; mRNA.
DR RefSeq; NP_001312911.1; NM_001325982.1.
DR AlphaFoldDB; G3CCC1; -.
DR SMR; G3CCC1; -.
DR STRING; 4097.G3CCC1; -.
DR GeneID; 107816701; -.
DR KEGG; ag:CCD33019; -.
DR KEGG; nta:107816701; -.
DR BioCyc; MetaCyc:MON18C3-48; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:1902246; P:cis-abienol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902242; P:copal-8-ol diphosphate(3-) catabolic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..792
FT /note="Cis-abienol synthase, chloroplastic"
FT /id="PRO_5000793117"
FT MOTIF 539..543
FT /note="DDXXD motif"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 792 AA; 91772 MW; DC0034030033395C CRC64;
MVLGLRSKII PLPDHKLGNI KLGSVTNAIC HRPCRVRCSH STASSMEEAK ERIRETFGKI
ELSPSSYDTA WVAMVPSRYS MNQPCFPQCL DWILENQRED GSWGLNPSHP LLVKDSLSST
LASLLALRKW RIGDNQVQRG LGFIETHGWA VDNKDQISPL GFEIIFPCMI NYAEKLNLDL
PLDPNLVNMM LCERELTIER ALKNEFEGNM ANVEYFAEGL GELCHWKEMM LRQRHNGSLF
DSPATTAAAL IYHQYDEKCF GYLNSILKLH DNWVPTICPT KIHSNLFLVD ALQNLGVDRY
FKTEVKRVLD EIYRLWLEKN EEIFSDVAHC AMAFRLLRMN NYEVSSEELE GFVDQEHFFT
TSSGKLMNHV AILELHRASQ VAIHERKDHI LDKISTWTRN FMEQKLLDKH IPDRSKKEME
FAMRKFYGTF DRVETRRYIE SYKMDSFKIL KAAYRSSGIN NIDLLKFSEH DFNLCQTRHK
EELQQMKRWF TDCKLEQVGL SQQYLYTSYF IIAAILFEPE YADARLAYAK YAIIITAVDD
FFDCFICKEE LQNIIELVER WEGYSTVGFR SERVRIFFLA LYKMVEEIAA KAETKQGRCV
KDHLINLWID MLKCMLVELD LWKIKSTTPS IEEYLSVACV TIGVPCFVLT SLYLLGPKLS
KDVIESSEVS ALCNCTAAVA RLINDIHSYK REQAESSTNM VSILITQSQG TISEEEAIRQ
IKEMMESKRR ELLGMVLQNK ESQLPQVCKD LFWTTINAAY SIHTHGDGYR FPEEFKNHIN
DVIYKPLNQY SP
