ATESY_VITVI
ID ATESY_VITVI Reviewed; 590 AA.
AC Q6PWU2; Q6PWU1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=(-)-alpha-terpineol synthase;
DE EC=4.2.3.111;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Gewuerztraminer;
RX PubMed=15184006; DOI=10.1016/j.phytochem.2004.03.018;
RA Martin D.M., Bohlmann J.;
RT "Identification of Vitis vinifera (-)-alpha-terpineol synthase by in silico
RT screening of full-length cDNA ESTs and functional characterization of
RT recombinant terpene synthase.";
RL Phytochemistry 65:1223-1229(2004).
CC -!- FUNCTION: Mediates the conversion of geranyl diphosphate into alpha-
CC terpineol, a monoterpenol. Monoterpenols contribute to the final grape
CC and wine aroma and flavor. Also forms some 1,8-cineole and traces of
CC other monoterpenoids. {ECO:0000269|PubMed:15184006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC EC=4.2.3.111; Evidence={ECO:0000269|PubMed:15184006};
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: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY572986; AAS79351.1; -; mRNA.
DR EMBL; AY572987; AAS79352.1; -; mRNA.
DR RefSeq; NP_001268216.1; NM_001281287.1.
DR AlphaFoldDB; Q6PWU2; -.
DR SMR; Q6PWU2; -.
DR GeneID; 100232956; -.
DR KEGG; vvi:100232956; -.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR OrthoDB; 401091at2759; -.
DR BRENDA; 4.2.3.111; 6671.
DR UniPathway; UPA00213; -.
DR ExpressionAtlas; Q6PWU2; baseline and differential.
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 Lyase; Magnesium; Metal-binding.
FT CHAIN 1..590
FT /note="(-)-alpha-terpineol synthase"
FT /id="PRO_0000418756"
FT MOTIF 339..343
FT /note="DDXXD motif"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 CONFLICT 126
FT /note="G -> S (in Ref. 1; AAS79352)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="S -> F (in Ref. 1; AAS79352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 68883 MW; CBF022DC6C614234 CRC64;
MALSMLSSIP NLITHTRLPI IIKSSSCKAS PRGIKVKIGN SNCEEIIVRR TANYHPTIWD
YDYVQSLRSD YVGETYTRRL DKLKRDVKPM LGKVKKPLDQ LELIDVLQRL GIYYHFKDEI
KRILNGIYNQ YNRHEEWQKD DLYATALEFR LLRQHGYDVP QDVFSRFKDD TGSFKACLCE
DMKGMLCLYE ASYLCVQGES TMEQARDFAH RHLGKGLEQN IDQNLAIEVK HALELPLHWR
MPRLEARWFI DVYEKRQDMN PILLEFAKLD FNMVQATHQE DLRHMSSWWS STRLGEKLNF
ARDRLMENFL WTVGVIFEPQ YGYCRRMSTK VNTLITIIDD VYDVYGTMDE LELFTDVVDR
WDINAMDPLP EYMKLCFLAL YNSTNEMAYD ALKEHGLHIV SYLRKAWSDL CKSYLLEAKW
YYSRYTPSLQ EYISNSWISI SGPVILVHAY FLVANPITKE ALQSLERYHN IIRWSSMILR
LSDDLGTSLD ELKRGDVPKS IQCYMYETGA SEEDARKHTS YLIGETWKKL NEDGAVESPF
PETFIGIAMN LARMAQCMYQ HGDGHGIEYG ETEDRVLSLL VEPIPSLSSE
