ATPSC_THYCA
ID ATPSC_THYCA Reviewed; 601 AA.
AC R4JQS2; R4JHV9; R4JQS8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 30.
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. C2; 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=R4JQS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=R4JQS2-2; Sequence=VSP_061123;
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; KC181096; AGK88251.1; -; Genomic_DNA.
DR EMBL; KC181101; AGK88256.1; -; mRNA.
DR EMBL; KC181104; AGK88259.1; -; mRNA.
DR SMR; R4JQS2; -.
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_0000453316"
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_061123"
FT CONFLICT 74
FT /note="D -> N (in Ref. 1; AGK88259)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="E -> K (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="I -> M (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> L (in Ref. 1; AGK88259)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> P (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="A -> V (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="K -> Q (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..241
FT /note="NEGRISDE -> DEGSISDG (in Ref. 1; AGK88259)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="S -> L (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="H -> R (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="V -> A (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="I -> V (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..306
FT /note="VSRG -> ASRW (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="NT -> YI (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="Y -> H (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..413
FT /note="LKDH -> FKDR (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="K -> Q (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 459..462
FT /note="ASLT -> GSLP (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="R -> Q (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 540..542
FT /note="GET -> REA (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="K -> E (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="D -> E (in Ref. 1; AGK88259)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="L -> I (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="F -> Y (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
FT CONFLICT 589..593
FT /note="HQHMG -> RQHVR (in Ref. 1; AGK88256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 69705 MW; C79E7D9B93B106AB CRC64;
MSTISIHHVG ILRNPLHSKS KRASINKPWS LSLPRSSSAS RLVEPCRVSS KTDTKPAEIT
RRSGNYEPSL WDFDFIQSLD NHHPYVKEEQ LKREEELIVQ VKILLGTKME AVKQLELIDD
LKNLGLSYFF RDEIKTILTS IYNNSFENKN NQVGDLYFTS LGFRLLRQHG FNVSQDIFDC
FKNEKGSDFD ETLIGEDTKA TLQLYEASFH LREGENTLEL ARQISTKYLQ KKVNEGRISD
ENLSSWIRHS LDLPLHWRIQ RLEARWFLDA YAVREDKNPL IFELAKLDFN IIQATQQEEL
KEVSRGWNDS CLAEKLPFVR DRVVESYFWG VGLFEGHEFG YQRKLTAANT LLISAIDDVY
DVYGTLDELR LFTDVFRRWD TESIDQLPYY MQLCYLALYN YVSGVAYDIL KDHRRNTIPY
LQETWVELVE AYMKEAEWYK SGYTPSLEEY LTIAKISIAS LTILLSVELS LPDSTIDRAT
FDRRHKMFYL SATVSRLADD LGTAPSELER GDVPKAIQCY MKDTNASEEE ARGHVRFMIG
ETWKELNTAM AKPDDCPFTE QVVEATANLG RAAQFIYREG DGHGHFQIHQ HMGNLFFHPY
V
