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SBPN2_PINBN
ID   SBPN2_PINBN             Reviewed;         627 AA.
AC   R9QMW5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=(-)-beta-pinene synthase 2, chloroplastic {ECO:0000303|PubMed:23679205};
DE            EC=4.2.3.120 {ECO:0000269|PubMed:23679205};
DE   AltName: Full=(-)-alpha-pinene synthase (-)betapin2, chloroplastic {ECO:0000303|PubMed:23679205};
DE            EC=4.2.3.119 {ECO:0000269|PubMed:23679205};
DE   AltName: Full=Terpene synthase (-)betapin2 {ECO:0000303|PubMed:23679205};
DE            Short=PbTPS-(-)betapin2 {ECO:0000303|PubMed:23679205};
DE   Flags: Precursor;
GN   Name=TPS-(-)Bpin2 {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 (-)-beta-pinene and, to a lower extent, to (-)-alpha-pinene
CC       (PubMed:23679205). {ECO:0000269|PubMed:23679205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate;
CC         Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.120;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25497;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate;
CC         Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.119;
CC         Evidence={ECO:0000269|PubMed:23679205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25489;
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; JQ240292; AFU73844.1; -; mRNA.
DR   BRENDA; 4.2.3.119; 4842.
DR   BRENDA; 4.2.3.120; 4842.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0018867; P:alpha-pinene metabolic process; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..627
FT                   /note="(-)-beta-pinene synthase 2, chloroplastic"
FT                   /id="PRO_0000455020"
FT   MOTIF           378..382
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   627 AA;  72004 MW;  456C985491BF2DB3 CRC64;
     MDLISVLPSA SKSCVCLHKP LSSSTHKLKP FCRKIRILGM PRPRKSVLMV SSMSISVNTL
     VSDDAVQRRT GGYHSNLWND DVIQFLSTPY GELAYRERAE RLIDEVRNIF SSMSLEDGES
     SDLIQRLWMV DNVERLGIDR HFKNEIKSAL DYVYSYWSQK GIGCGTKSII TDLNSTALGF
     RILRLHGYPV SAEVFKHFRN QIGQFVSCHS ETEEDIRSIV NLYRASLIAF PGEKVMEEAE
     IFSEKYLKET LQKIPDCSLS REIGDVLEHG WHTNLPRFEA RNYMDVFGQD TKNMESNRKA
     EKLLELAKLE FNIFQSIQKT ELESLLRWWN DSGSPQITFT RHRHVEYYTL ASCIAFEPQH
     SGFRLGFAKA CHIITVLDDM YDLFGTVEEL KLFTAAIKRW DPSATDCLPQ YMKGIYMMVY
     NTVNEMSAEA QKAQRRDTLN YARQAWEVYL DSYMQEAKWI ATGYLPTFEE YLENGKVSSG
     HRVSALQPML TMDIPFPPHI LKEVDFPSNL NDLACAILRL RGDTRCYQED RARGEETSCI
     SCYMKDNPGA TEEDALNHLN VMISGVIKEL NWELLKPDSS VPISSKKINF DITRAFHYGY
     KYRDGYSVSS VETKSLVMRT LLEPVPL
 
 
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