SBHS6_THYVU
ID SBHS6_THYVU Reviewed; 603 AA.
AC L0HAM7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Sabinene hydrate synthase, chloroplastic {ECO:0000303|PubMed:23246843};
DE EC=4.2.3.11 {ECO:0000269|PubMed:23246843};
DE AltName: Full=Terpene synthase 6 {ECO:0000303|PubMed:23246843};
DE Short=TvTPS6 {ECO:0000303|PubMed:23246843};
DE Flags: Precursor;
GN Name=TPS6 {ECO:0000303|PubMed:23246843};
OS Thymus vulgaris (Thyme).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Thymus.
OX NCBI_TaxID=49992;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ASN-350, CATALYTIC
RP ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23246843; DOI=10.1016/j.abb.2012.12.003;
RA Krause S.T., Koellner T.G., Asbach J., Degenhardt J.;
RT "Stereochemical mechanism of two sabinene hydrate synthases forming
RT antipodal monoterpenes in thyme (Thymus vulgaris).";
RL Arch. Biochem. Biophys. 529:112-121(2013).
CC -!- FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural
CC products (PubMed:23246843). Monoterpene synthase which catalyzes the
CC conversion of geranyl diphosphate (GPP) to sabinene hydrate, mainly
CC (Z)-sabinene hydrate and to a lower extent (E)-sabinene hydrate, and
CC the formation of minor amounts and traces of several other monoterpenes
CC (e.g. mainly alpha-thujene, alpha-pinene and myrcene)
CC (PubMed:23246843). {ECO:0000269|PubMed:23246843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = diphosphate + sabinene
CC hydrate; Xref=Rhea:RHEA:19565, ChEBI:CHEBI:15377, ChEBI:CHEBI:16377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.11;
CC Evidence={ECO:0000269|PubMed:23246843};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19566;
CC Evidence={ECO:0000269|PubMed:23246843};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:E2E2P0};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:E2E2P0};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:E2E2P0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.5 uM for geranyl diphosphate {ECO:0000269|PubMed:23246843};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:23246843}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0M3Q1Q3}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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|UniProtKB:Q9X839}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JX946357; AGA96119.1; -; mRNA.
DR SMR; L0HAM7; -.
DR BRENDA; 4.2.3.11; 12984.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0050469; F:sabinene-hydrate synthase activity; IEA:UniProtKB-EC.
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; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..603
FT /note="Sabinene hydrate synthase, chloroplastic"
FT /id="PRO_0000453312"
FT REGION 363..369
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT REGION 435..472
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT MOTIF 357..361
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9X839"
FT BINDING 357
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 357
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 501
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 509
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT SITE 350
FT /note="Confers reaction mechanism stereospecificity"
FT /evidence="ECO:0000269|PubMed:23246843"
FT MUTAGEN 350
FT /note="N->I: Lossed ability to produce (Z)-sabinene hydrate
FT but increased ability to produce (E)-sabinene from geranyl
FT diphosphate (GPP)."
FT /evidence="ECO:0000269|PubMed:23246843"
SQ SEQUENCE 603 AA; 70062 MW; B2338856D5283F83 CRC64;
MSTISINHVG LLRNPLHGKS KRASINKSWS LCLPRSSSAS RLVKPCRVSS KTDTKPAEMT
RRSGNYEPSL WDFDFIQSLD NHHPHVKEKQ LKREEELIVE VKMLLGTKIE AVKQLELIDD
LKNLGLSYFF RDEIKMVLTS IYNNFFENKN NQVGDLYFTA LGFRLLRQHG FNVSQEIFDC
FKNEKGSDFD ETLIGEDTKA TLQLYEASFH LREGENTLEL ARQISTKYLQ KKVDEGSIND
ENLSSWIRHS LDLPLHWRIQ RLEARWFLDA YAAREDKNPL IFELTKLDFN IIQATQQEEL
KEVSRWWNNS RLAEKLPFVR DRVVECYFWA VGLFDGHDYG FQRKVNAAVN ILITAIDDVY
DVYGTLDELR LFTDVIRRWD TQSIDQLPYY MQLCYLTLYN YVSDLAYNIL KDRGINTIPH
LHQSWVNTVE AYLKEAEWYE SGYAPSLEEY LSIASISIGV IPIVIPLEVS IPNSTFHRRS
PFEYHRYDIL HLSAMVLRLA DDLGTAQYEV ETGDVPKAVQ CYIKDTNASE EEAREHVRFM
IGEVWKELNT AMAESDDCPF TEQGAWAAVN IGRAAQFIYL EGDGHGRFQI HQHMENLFFH
PCV
