GTPS3_THYVU
ID GTPS3_THYVU Reviewed; 596 AA.
AC K9Y645;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Putative terpene synthase 3, chloroplastic {ECO:0000305};
DE Short=TvTPS3 {ECO:0000305};
DE EC=4.2.3.- {ECO:0000250|UniProtKB:E2E2P0};
DE AltName: Full=Probably inactive gamma-terpinene synthase {ECO:0000305|Ref.1};
DE Flags: Precursor;
GN Name=TPS3 {ECO:0000305}; Synonyms=GTS {ECO:0000303|Ref.1};
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.
CC -!- FUNCTION: Putative monoterpene synthase.
CC {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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JQ957866; AFZ41788.1; -; mRNA.
DR SMR; K9Y645; -.
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 3, chloroplastic"
FT /id="PRO_0000453311"
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"
SQ SEQUENCE 596 AA; 69098 MW; BC409AC8B02593E6 CRC64;
MATLSMQVST LSKQVKNLNT FGMGSASKLP MVARRVSTIR LRPICSASLQ VEEKTRRSGN
YQAPVWNNDF IQSFSTDKYK DEKFLKKKEE LIAQVKILLN TKMEAVKQLE LIEDLRNLGL
TYYFEDEFKK ILTSIYNEHK GFKNEQVGDL YFTSLAFRLL RLHGFDVSED VFNFFKNEDG
SDFKASLGEN TKDVLELYEA SFLIRVGEVT LEQARVFSTK ILEKKVEEGI KDEKLLAWIQ
HSLALPLHWR IQRLEARWFL DAYKARKDMN PIIFELGKID FHIIQETQLQ EVQEVSQWWT
NTNLAEKLPF VRDRIVECYF WALGLFEPHE YGYQRKMAAI IITFVTIIDD VYDVYGTLDE
LQLFTDAIRT WDFESISTLP YYMQVCYLAL YTYASELAYD ILKDQGFNSI SYLQRSWLSL
VEGFFQEAKW YYAGYTPTLA EYLENAKVSI SSPTIISQVY FTLPNSTERT VVENVYGYHN
ILYLSGMILR LADDLGTTQF ELKRGDVQKA IQCYMNDNNA TEQEGTEHVK YLLREAWQEM
NSAMADPDCP LSEDLVFAAA NLGRASQFIY LDGDGHGVQH SEIHNQMGGL IFEPYV
