位置:首页 > 蛋白库 > FARNS_PICXS
FARNS_PICXS
ID   FARNS_PICXS             Reviewed;         580 AA.
AC   F2XF99;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=(E,E)-alpha-farnesene synthase {ECO:0000303|PubMed:21385377};
DE            EC=4.2.3.46 {ECO:0000269|PubMed:21385377};
DE   AltName: Full=(E)-beta-ocimene synthase {ECO:0000303|PubMed:21385377};
DE            EC=4.2.3.106 {ECO:0000269|PubMed:21385377};
DE   AltName: Full=Terpene synthase TPS-Far/Oci {ECO:0000303|PubMed:21385377};
DE            Short=PgxeTPS-Far/Oci {ECO:0000303|PubMed:21385377};
GN   Name=TPS-Far/Oci {ECO:0000303|PubMed:21385377};
OS   Picea engelmannii x Picea glauca (Hybrid white spruce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=373101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP   FAMILY.
RC   STRAIN=cv. Fa1-1028;
RX   PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA   Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA   Dullat H.K., Bohlmann J.;
RT   "Transcriptome mining, functional characterization, and phylogeny of a
RT   large terpene synthase gene family in spruce (Picea spp.).";
RL   BMC Plant Biol. 11:43-43(2011).
CC   -!- FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of
CC       sesquiterpene and monoterpene natural products included in conifer
CC       oleoresin secretions and volatile emissions; these compounds contribute
CC       to biotic and abiotic stress defense against herbivores and pathogens
CC       (PubMed:21385377). Catalyzes the conversion of (2E,6E)-farnesyl
CC       diphosphate (FPP) to (3E,6E)-alpha-farnesene and of (2E)-geranyl
CC       diphosphate (GPP) to (E)-beta-ocimene (PubMed:21385377).
CC       {ECO:0000269|PubMed:21385377}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC         diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
CC         Evidence={ECO:0000269|PubMed:21385377};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC         Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:64280; EC=4.2.3.106;
CC         Evidence={ECO:0000269|PubMed:21385377};
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:21385377}.
CC   -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:21385377}.
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:A0A1C9J6A7}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ426157; ADZ45514.1; -; mRNA.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:UniProtKB.
DR   GO; GO:0052578; F:alpha-farnesene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016106; P:sesquiterpenoid 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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..580
FT                   /note="(E,E)-alpha-farnesene synthase"
FT                   /id="PRO_0000454400"
FT   MOTIF           331..335
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         331
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         331
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         335
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         335
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         483
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   580 AA;  66198 MW;  CA1FC9292AE8CEAC CRC64;
     MASVDQSQLC SKSVSMSLSV DDGVQRRTGD YHSNLWDDDF IQSLSTPYGA PCYRERAERL
     IGEVKEMFNS VRLSPLNDLL QGLSMVDSVE RLGIDRHFKN EIKSALDYVY SYWSEKGIGC
     GRESVVTDLN SSALGFRALR LHGYPVSSDV FKDQNGQFAC SANTQTEGEM RGVLNLFRAS
     LVAFPGEKVM EDAERFSAIY LKEALKTVPI CSGSLSGEIE YVLEYGWLTN FPRLEARNYI
     DIFGKDTSPC LQTEKLLELA KLEFNIFHSL QQRELKQVSR WWKDSGFSQL TFTRHRHVEF
     YTLASCIAIE PKHSAFRLGF AKLCYLGIVL DDIYDTFGTM DELELFTAAI KRWDPSATEC
     LPEYMKGVYM VFYECVNQMA REAEKTQGRD TLSYARNTWE AVFDAFLEEA KWISSGYIPT
     FEEYLENGKV SFGYRAATLQ PILTLDVPLP LHILQEIDFP SRFNDLAASI LRLRGDVCGY
     KAERSRGEEA SSISCYMKDN PGATEEDALN QIDTMIKEKI KELNWEFLKP DSNVPISSKK
     HAFDILRAFY HLYKYRDGFS IANNETKSLV MRTLLETVPF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024