SBHS7_THYVU
ID SBHS7_THYVU Reviewed; 597 AA.
AC L0HB77;
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=(E)-sabinene hydrate synthase, chloroplastic {ECO:0000303|PubMed:23246843};
DE EC=4.2.3.11 {ECO:0000269|PubMed:23246843};
DE AltName: Full=Terpene synthase 7 {ECO:0000303|PubMed:23246843};
DE Short=TvTPS7 {ECO:0000303|PubMed:23246843};
DE Flags: Precursor;
GN Name=TPS7 {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 ILE-346, 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,
CC specifically (E)-sabinene hydrate, and the formation of minor amounts
CC and traces of several other monoterpenes (e.g. mainly alpha-pinene,
CC limonene and alpha-terpineol) (PubMed:23246843).
CC {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=6.1 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; JX946358; AGA96120.1; -; mRNA.
DR SMR; L0HB77; -.
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..597
FT /note="(E)-sabinene hydrate synthase, chloroplastic"
FT /id="PRO_0000453313"
FT REGION 359..365
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT REGION 431..468
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT MOTIF 353..357
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9X839"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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 495
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 503
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT SITE 346
FT /note="Confers reaction mechanism stereospecificity"
FT /evidence="ECO:0000269|PubMed:23246843"
FT MUTAGEN 346
FT /note="I->N: Reduced ability to produce (E)-sabinene
FT hydrate but acquired ability to produce (Z)-sabinene from
FT geranyl diphosphate (GPP)."
FT /evidence="ECO:0000269|PubMed:23246843"
SQ SEQUENCE 597 AA; 69225 MW; 4334E5A2368E69DD CRC64;
MSTISINHVG ILRNPLQCKN KRTSINKPWS LSLPRSSPAS RLVKPCRVSS KVDTMPDEIT
RRSGNYEPSL WDLDFIQSLD NHHPYVKEMQ LKREEELIVQ VKMLLGTKME AVKQLELIDD
LKNLGLSYFF RDEIKTILTS IYNNSFENNN QVGDLYFTAL GFRLLRQHGF NVSQQIFDCF
KDNDFDETLI GEDTKGILQL YEASFHLREG ENTLELARQI STKYLQKKVD EGSINDENLS
SWIRHSLDLP LHWRIQRLEA RCFLDAYAAR EDKNPLIFKL AELDFNIIQA TQQQELKEIS
RWWNDSSLAE KLPFVRDRVV ECYFWAVGLF EGHEFGFQRK ITAAIIILIT AIDDVYDVYG
TLDELQLFTD VIRRWDTQSI DQLPYYMQLC YLALYNFVSD LAYDILKDRG LNTIPYLHRS
WVELVEAYLK EAGWYENGYT PSLEEYLTNA TISIGVPPIV LPVEVSLPNS TIHRTQFDRP
HKILDLSARV LRLADDLGTA SSELERGDVP KAIQCYMKDN NASEEEAREH VRFMIREAWK
ELNTAMAEPD NCPFTEQTVE AAANLGRAAQ FIYLEGDGHA HFQIHQHLEN LFFHPCV
