SCS_SALOF
ID SCS_SALOF Reviewed; 591 AA.
AC O81191;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=1,8-cineole synthase, chloroplastic;
DE Short=SCS;
DE EC=4.2.3.108;
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 1,8-cineole from geranyl
CC diphosphate. The enzyme also produces significant amounts of (+)- and
CC (-)-alpha-pinene, (+)- and (-)-beta-pinene, myrcene and (+)-sabinene.
CC {ECO:0000269|PubMed:9614092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate;
CC Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108;
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 -!- 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; AF051899; AAC26016.1; -; mRNA.
DR AlphaFoldDB; O81191; -.
DR SMR; O81191; -.
DR PRIDE; O81191; -.
DR KEGG; ag:AAC26016; -.
DR BRENDA; 4.2.3.108; 5564.
DR SABIO-RK; O81191; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102313; F:1,8-cineole 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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..591
FT /note="1,8-cineole synthase, chloroplastic"
FT /id="PRO_0000033635"
FT MOTIF 345..349
FT /note="DDXXD motif"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 591 AA; 69369 MW; 575F5C8A62C82D8B CRC64;
MSSLIMQVVI PKPAKIFHNN LFSVISKRHR FSTTITTRGG RWAHCSLQMG NEIQTGRRTG
GYQPTLWDFS TIQLFDSEYK EEKHLMRAAG MIAQVNMLLQ EEVDSIQRLE LIDDLRRLGI
SCHFDREIVE ILNSKYYTNN EIDESDLYST ALRFKLLRQY DFSVSQEVFD CFKNDKGTDF
KPSLVDDTRG LLQLYEASFL SAQGEETLHL ARDFATKFLH KRVLVDKDIN LLSSIERALE
LPTHWRVQMP NARSFIDAYK RRPDMNPTVL ELAKLDFNMV QAQFQQELKE ASRWWNSTGL
VHELPFVRDR IVECYYWTTG VVERREHGYE RIMLTKINAL VTTIDDVFDI YGTLEELQLF
TTAIQRWDIE SMKQLPPYMQ ICYLALFNFV NEMAYDTLRD KGFNSTPYLR KAWVDLVESY
LIEAKWYYMG HKPSLEEYMK NSWISIGGIP ILSHLFFRLT DSIEEEDAES MHKYHDIVRA
SCTILRLADD MGTSLDEVER GDVPKSVQCY MNEKNASEEE AREHVRSLID QTWKMMNKEM
MTSSFSKYFV QVSANLARMA QWIYQHESDG FGMQHSLVNK MLRGLLFDRY E
