SSS_SALOF
ID SSS_SALOF Reviewed; 590 AA.
AC O81193;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=(+)-sabinene synthase, chloroplastic;
DE Short=SSS;
DE EC=4.2.3.110;
DE Flags: Precursor;
OS Salvia officinalis (Sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=38868;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9614092; DOI=10.1074/jbc.273.24.14891;
RA Wise M.L., Savage T.J., Katahira E., Croteau R.;
RT "Monoterpene synthases from common sage (Salvia officinalis). cDNA
RT isolation, characterization, and functional expression of (+)-sabinene
RT synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase.";
RL J. Biol. Chem. 273:14891-14899(1998).
CC -!- FUNCTION: Catalyzes the formation of the (-)-3-isothujone precursor
CC sabinene from geranyl diphosphate. The enzyme also produces significant
CC amounts of gamma-terpinene, terpinolene and limonene.
CC {ECO:0000269|PubMed:9614092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-sabinene + diphosphate;
CC Xref=Rhea:RHEA:32547, ChEBI:CHEBI:33019, ChEBI:CHEBI:50029,
CC ChEBI:CHEBI:58057; EC=4.2.3.110;
CC Evidence={ECO:0000269|PubMed:9614092};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Terpene metabolism; sabinene hydrate biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AF051901; AAC26018.1; -; mRNA.
DR AlphaFoldDB; O81193; -.
DR SMR; O81193; -.
DR KEGG; ag:AAC26018; -.
DR BRENDA; 4.2.3.108; 5564.
DR BRENDA; 4.2.3.110; 5564.
DR BRENDA; 4.2.3.114; 5564.
DR SABIO-RK; O81193; -.
DR UniPathway; UPA00731; -.
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: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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..590
FT /note="(+)-sabinene synthase, chloroplastic"
FT /id="PRO_0000033621"
FT MOTIF 343..347
FT /note="DDXXD motif"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 590 AA; 68942 MW; 3E9CDFEDA2F0307D CRC64;
MSSISINIAM PLNSLHNFER KPSKAWSTSC TAPAARLRAS SSLQQEKPHQ IRRSGDYQPS
LWDFNYIQSL NTPYKEQRHF NRQAELIMQV RMLLKVKMEA IQQLELIDDL QYLGLSYFFQ
DEIKQILSSI HNEPRYFHNN DLYFTALGFR ILRQHGFNVS EDVFDCFKIE KCSDFNANLA
QDTKGMLQLY EASFLLREGE DTLELARRFS TRSLREKFDE GGDEIDEDLS SWIRHSLDLP
LHWRVQGLEA RWFLDAYARR PDMNPLIFKL AKLNFNIVQA TYQEELKDIS RWWNSSCLAE
KLPFVRDRIV ECFFWAIAAF EPHQYSYQRK MAAVIITFIT IIDDVYDVYG TIEELELLTD
MIRRWDNKSI SQLPYYMQVC YLALYNFVSE RAYDILKDQH FNSIPYLQRS WVSLVEGYLK
EAYWYYNGYK PSLEEYLNNA KISISAPTII SQLYFTLANS IDETAIESLY QYHNILYLSG
TILRLADDLG TSQHELERGD VPKAIQCYMN DTNASEREAV EHVKFLIREA WKEMNTVTTA
SDCPFTDDLV AAAANLARAA QFIYLDGDGH GVQHSEIHQQ MGGLLFQPYV
