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GTPS2_THYVU
ID   GTPS2_THYVU             Reviewed;         596 AA.
AC   K9Y6Y9; A0A5P8U4C2; K9Y851; V5JZJ2;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Putative terpene synthase 2, chloroplastic {ECO:0000303|PubMed:26750479, ECO:0000303|PubMed:31644985};
DE            Short=TTPS2 {ECO:0000303|PubMed:31644985};
DE            Short=TvTPS2 {ECO:0000303|PubMed:26750479};
DE            EC=4.2.3.- {ECO:0000250|UniProtKB:E2E2P0};
DE   AltName: Full=Inactive gamma-terpinene synthase 2, chloroplastic {ECO:0000303|PubMed:26750479};
DE   Flags: Precursor;
GN   Name=TPS2 {ECO:0000303|PubMed:26750479, ECO:0000303|PubMed:31644985};
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].
RC   TISSUE=Leaf;
RA   Rudolph K., Schweininger J., Mueller-Uri F., Kreis W.;
RT   "Gamma-terpinene synthase from Thymus vulgaris (GTS).";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schimmel J., Krause S.T., Asbach J., Degenhardt J.;
RT   "Chemotype regulation in thyme (Thymus vulgaris) is based on terpene
RT   synthase expression patterns.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=26750479; DOI=10.1107/s2053230x15023043;
RA   Rudolph K., Parthier C., Egerer-Sieber C., Geiger D., Muller Y.A.,
RA   Kreis W., Mueller-Uri F.;
RT   "Expression, crystallization and structure elucidation of gamma-terpinene
RT   synthase from Thymus vulgaris.";
RL   Acta Crystallogr. F Struct. Biol. Commun. 72:16-23(2016).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=31644985; DOI=10.1016/j.phytochem.2019.112126;
RA   Tohidi B., Rahimmalek M., Arzani A., Trindade H.;
RT   "Sequencing and variation of terpene synthase gene (TPS2) as the major gene
RT   in biosynthesis of thymol in different Thymus species.";
RL   Phytochemistry 169:112126-112126(2020).
CC   -!- FUNCTION: Putative monoterpene synthase inactive on geranyl diphosphate
CC       (GPP). {ECO:0000250|UniProtKB:E2E2P0}.
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   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000250|UniProtKB:E2E2P0}.
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   -!- MISCELLANEOUS: Missing Asp-356 and Thr-565 residues essential for
CC       gamma-terpinene synthase activity. {ECO:0000269|PubMed:26750479}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; JQ957865; AFZ41787.1; -; mRNA.
DR   EMBL; JX997981; AGS42395.1; -; mRNA.
DR   EMBL; JQ957864; AFZ41786.1; -; mRNA.
DR   EMBL; MH686200; QFS22625.1; -; mRNA.
DR   SMR; K9Y6Y9; -.
DR   BRENDA; 4.2.3.114; 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: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   2: Evidence at transcript level;
KW   Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..596
FT                   /note="Putative terpene synthase 2, chloroplastic"
FT                   /id="PRO_0000453310"
FT   REGION          355..361
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT   REGION          427..464
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT   MOTIF           349..353
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X839"
FT   BINDING         349
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         349
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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         493
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
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   CONFLICT        3
FT                   /note="T -> S (in Ref. 2; AGS42395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="T -> I (in Ref. 1; AFZ41787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="E -> K (in Ref. 1; AFZ41787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="F -> Y (in Ref. 2; AGS42395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="F -> L (in Ref. 2; AGS42395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="E -> Q (in Ref. 4; QFS22625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   596 AA;  69023 MW;  06B5CE3F4EB93A98 CRC64;
     MATLSMQVST LSKQVKNLNT FGMGSASKLP MVARRVSTTR LRPICSASLQ VEEETRRSGN
     YQAPVWNNDF IQSFSTDKYK DEKFLKKKEE LIAQVKVLLN TKMEAVKQLE LIEDLRNLGL
     TYYFEDEFKK ILTSIYNEHK GFKNEQVGDL YFTSLAFRLL RLHGFDVSED VFNFFKNEDG
     SDFKASLGEN TKDVLELYEA SFLIRVGEVT LEQARVFSTK ILEKKVEEGI KDEKLLAWIQ
     HSLALPLHWR IQRLEARWFL DAYKARKDMN PIIYELGKID FHIIQETQLQ EVQEVSQWWT
     NTNLAEKLPF VRDRIVECYF WALGLFEPHE YGYQRKMAAI IITFVTIIDD VYDVYGTLDE
     LQLFTDAIRK WDVESISTLP YYMQVCYLAV FTYASELAYD ILKDQGFNSI SYLQRSWLSL
     VEGFFQEAKW YYAGYTPTLA EYLENAKVSI SSPTIISQVY FTLPNSTERT VVENVFGYHN
     ILYLSGMILR LADDLGTTQF ELKRGDVQKA IQCYMNDNNA TEEEGTEHVK YLLREAWQEM
     NSAMADPDCP LSEDLVFAAA NLGRASQFIY LDGDGHGVQH SEIHNQMGGL IFEPYV
 
 
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