ATPS3_THYCA
ID ATPS3_THYCA Reviewed; 601 AA.
AC R4JJJ1; R4JND2; R4JNE4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Alpha-terpineol synthase, chloroplastic {ECO:0000303|PubMed:23624978};
DE EC=4.2.3.- {ECO:0000269|PubMed:23624978};
DE AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:23624978};
DE Short=TcTPS5 {ECO:0000303|PubMed:23624978};
DE Flags: Precursor;
GN Name=TPS5 {ECO:0000303|PubMed:23624978};
OS Thymus caespititius (Cretan thyme) (Origanum caespititium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Thymus.
OX NCBI_TaxID=751871;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. 319; TISSUE=Flower;
RX PubMed=23624978; DOI=10.1007/s00425-013-1884-2;
RA Lima A.S., Schimmel J., Lukas B., Novak J., Barroso J.G., Figueiredo A.C.,
RA Pedro L.G., Degenhardt J., Trindade H.;
RT "Genomic characterization, molecular cloning and expression analysis of two
RT terpene synthases from Thymus caespititius (Lamiaceae).";
RL Planta 238:191-204(2013).
CC -!- FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural
CC products (PubMed:23624978). Monoterpene synthase which catalyzes the
CC conversion of geranyl diphosphate (GPP) to alpha-terpineol (isomer is
CC not determined) (PubMed:23624978). {ECO:0000269|PubMed:23624978}.
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 Evidence={ECO:0000269|PubMed:23624978};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552;
CC Evidence={ECO:0000269|PubMed:23624978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (R)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32555, ChEBI:CHEBI:300,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC Evidence={ECO:0000269|PubMed:23624978};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32556;
CC Evidence={ECO:0000269|PubMed:23624978};
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:0000269|PubMed:23624978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0M3Q1Q3}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=R4JJJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=R4JJJ1-2; Sequence=VSP_061124;
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; KC181095; AGK88250.1; -; Genomic_DNA.
DR EMBL; KC181102; AGK88257.1; -; mRNA.
DR EMBL; KC181105; AGK88260.1; -; mRNA.
DR SMR; R4JJJ1; -.
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 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Lyase; Magnesium; Manganese;
KW Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..601
FT /note="Alpha-terpineol synthase, chloroplastic"
FT /id="PRO_0000453317"
FT REGION 363..369
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT REGION 435..471
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 499
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 507
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT VAR_SEQ 1..46
FT /note="MSTISIHHVGILRNPLHSKSKRASINKPWSLSLPRSSSASRLVEPC -> M
FT (in isoform 2)"
FT /id="VSP_061124"
FT CONFLICT 123
FT /note="N -> D (in Ref. 1; AGK88257)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="L -> P (in Ref. 1; AGK88257)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="D -> Y (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="V -> A (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="E -> G (in Ref. 1; AGK88257)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..234
FT /note="QVN -> KVD (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="L -> S (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> V (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="K -> E (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="K -> E (in Ref. 1; AGK88260)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="C -> R (in Ref. 1; AGK88257)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="YI -> DT (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="R -> S (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="H -> Y (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="Q -> E (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 459..462
FT /note="GSLP -> ASLT (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="Q -> R (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 540..542
FT /note="REA -> GET (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="V -> A (in Ref. 1; AGK88257)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="I -> L (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="Y -> F (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 589..593
FT /note="RQHVR -> HQHMG (in Ref. 1; AGK88250)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="F -> L (in Ref. 1; AGK88260)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 70037 MW; E4F2F69C74B900FF CRC64;
MSTISIHHVG ILRNPLHSKS KRASINKPWS LSLPRSSSAS RLVEPCRVSS KTDTKPAEIT
RRSGNYEPSL WDFDFIQSLD NHHPYVKEKQ LKREEELIVQ VKMLLGTKME AVKQLELIDD
LKNLGLSYFF RDEIKTILTS IYNNSFENKN NQVGDLYFTS LGFRLLRQHG FNVSQDIFDC
FKNEKGSDFD ETLIGEDTKA TLQLYEVSFH LREGENTLEL ARQISTKYLQ KQVNEGRISD
ENLSLWIRHS LDLPLHWRIQ RLEARWFLDA YAAREDKNPL IFKLAKLDFN IIQATQQEEL
KEVSRWWNDS CLAEKLPFVR DRVVESYFWG VGLFEGHEFG YQRKLTAAYI LLISAIDDVY
DVYGTLDELR LFTDVFRRWD TESIDQLPYY MQLCYLALHN YVSGVAYDIL KDHRRNTIPY
LQETWVELVE AYMKEAEWYQ SGYTPSLEEY LTIAKISIGS LPILLSVELS LPDSTIDRAT
FDRRHKMFYL SATVSRLADD LGTAPSELER GDVPKAIQCY MKDTNASEEE AQGHVRFMIR
EAWKELNTAM AEPDDCPFTE QVVEATANIG RAAQYIYREG DGHGHFQIRQ HVRNLFFHPY
V
