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ATERP_PINBN
ID   ATERP_PINBN             Reviewed;         626 AA.
AC   R9QMR5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Alpha terpineol synthase, chloroplastic {ECO:0000303|PubMed:23679205};
DE            EC=4.2.3.111 {ECO:0000269|PubMed:23679205};
DE            EC=4.2.3.112 {ECO:0000269|PubMed:23679205};
DE   AltName: Full=(-)-limonene synthase, chloroplastic {ECO:0000303|PubMed:23679205};
DE            EC=4.2.3.16 {ECO:0000269|PubMed:23679205};
DE   AltName: Full=Geraniol synthase, chloroplastic {ECO:0000303|PubMed:23679205};
DE            EC=3.1.7.11 {ECO:0000269|PubMed:23679205};
DE   AltName: Full=Terpene synthase alphaterp {ECO:0000303|PubMed:23679205};
DE            Short=PbTPS-alphaterp {ECO:0000303|PubMed:23679205};
DE   AltName: Full=Terpinolene synthase, chloroplastic {ECO:0000303|PubMed:23679205};
DE            EC=4.2.3.113 {ECO:0000269|PubMed:23679205};
DE   Flags: Precursor;
GN   Name=TPS-Aterp {ECO:0000303|PubMed:23679205};
OS   Pinus banksiana (Jack pine) (Pinus divaricata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=23679205; DOI=10.1186/1471-2229-13-80;
RA   Hall D.E., Yuen M.M.S., Jancsik S., Quesada A.L., Dullat H.K., Li M.,
RA   Henderson H., Arango-Velez A., Liao N.Y., Docking R.T., Chan S.K.,
RA   Cooke J.E.K., Breuil C., Jones S.J.M., Keeling C.I., Bohlmann J.;
RT   "Transcriptome resources and functional characterization of monoterpene
RT   synthases for two host species of the mountain pine beetle, lodgepole pine
RT   (Pinus contorta) and jack pine (Pinus banksiana).";
RL   BMC Plant Biol. 13:80-80(2013).
CC   -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC       monoterpene natural products included in conifer oleoresin secretions
CC       and volatile emissions; these compounds contribute to biotic and
CC       abiotic stress defense against herbivores and pathogens
CC       (PubMed:23679205). Catalyzes the conversion of (2E)-geranyl diphosphate
CC       (GPP) to (-)-alpha-terpineol, (+)-alpha-terpineol and terpin-4-ol, and,
CC       to a lower extent, to geraniol, terpinolene and (-)-limonene
CC       (PubMed:23679205). {ECO:0000269|PubMed:23679205}.
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:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552;
CC         Evidence={ECO:0000269|PubMed:23679205};
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         EC=4.2.3.112; Evidence={ECO:0000269|PubMed:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32556;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate;
CC         Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC         Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.113;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC         Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.16;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC       {ECO:0000269|PubMed:23679205}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:23679205}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000305}.
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DR   EMBL; JQ240308; AFU73860.1; -; mRNA.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050552; F:(4S)-limonene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:1903448; P:geraniol biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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   Chloroplast; Hydrolase; Lyase; Magnesium; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..626
FT                   /note="Alpha terpineol synthase, chloroplastic"
FT                   /id="PRO_0000455017"
FT   MOTIF           377..381
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         381
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         381
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         529
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   626 AA;  71948 MW;  B1CCA7CFCB57100F CRC64;
     MALLSVAPLA SKSRLHKTLI TSAHHLKPSP TTIPTLPVCT RRKTFTASIT MCLTAPVSDD
     GVKRRIGNHH SNLWDHDFIL SLSTPYEAPS YRERAARLIS EVKEMFTEIE DGLSITPLND
     LLSRLSMVDS IERLGVDRHF KMEIKSALDY VHRYWSEKGI GCGRESGVTD LNSTALGLRT
     LRLHGYPVSS SVLEQFKDEK GQFATSSIQT DPGEIRTIFN LFRASLVAFP NEKVMEDAQI
     FSTIYLKEYL EKIPLSSLSR QIEYVMEYGW HTNLPRLEAR HYMDVFGDNE MPWMSYVNTE
     KLLELAKLEF NIFHSIQQRE LKHISRWWKD SGFSQMNFVR HRHVEYYTLA SCFAIDPEHS
     AFRVSFAKMC HLGTVLDDIY DTFGTMEELQ LFTAAVKRWD PSATDSLPEY MKRVYTVLYE
     TVNEMAQVAK KSQGRDTINY ARHAWEAYLD SYMKEAEWIS TGCLPTFEEY YENGKISFGY
     RICMLQPILS MDIPFPHHIL QEIDYPSRFS SLAAGILRLK GDTRCYQADS ARGEEASCIS
     CYMKENPGLT EEDVVNHIHG MVDDLIKELN WELLKPDCNV PISSKKHAFD ICRAFHHGYK
     YRDGYSVATN EIKDLVMITV LEPVPL
 
 
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