位置:首页 > 蛋白库 > CINES_PICSI
CINES_PICSI
ID   CINES_PICSI             Reviewed;         612 AA.
AC   C0PT35;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=1,8-cineole synthase, chloroplastic {ECO:0000303|PubMed:21385377};
DE            EC=4.2.3.108 {ECO:0000269|PubMed:21385377};
DE   AltName: Full=Terpene synthase TPS-Cin {ECO:0000303|PubMed:21385377};
DE            Short=PsTPS-Cin {ECO:0000303|PubMed:21385377};
DE   Flags: Precursor;
GN   Name=TPS-Cin {ECO:0000303|PubMed:21385377};
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. FB3-425; TISSUE=Bark;
RX   PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA   Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA   Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA   Douglas C.J., Ritland K., Bohlmann J.;
RT   "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT   high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT   sitchensis).";
RL   BMC Genomics 9:484-484(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP   FAMILY.
RC   STRAIN=cv. FB3-425;
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       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:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate
CC       (GPP) to 1,8-cineole (PubMed:21385377). {ECO:0000269|PubMed:21385377}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate;
CC         Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108;
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   -!- 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: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; BT071518; ACN40975.1; -; mRNA.
DR   EMBL; HQ426165; ADZ45499.1; -; mRNA.
DR   OMA; INSIQCY; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0102313; F:1,8-cineole 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:0010333; F:terpene synthase activity; 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   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..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..612
FT                   /note="1,8-cineole synthase, chloroplastic"
FT                   /id="PRO_0000454401"
FT   MOTIF           363..367
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         515
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   612 AA;  70287 MW;  94F04B9CD51B91E3 CRC64;
     MALVSVAPLA SRSCLSKSLI SSTHELKPLR RTILPTLRWK SATPSINMCL TTSNSVDAVQ
     RRIANHHSNL WDDDFIQSLS TPYEAPSYRE RAERLIGEVK EMFESMGPNN DLLQRLSMVE
     SVERLGIDRH FKNEIKSALD YVYSHWNEKG IGCGRDSVVS DLNSTALALR TLRLHGYPVS
     SDVLEHFKDQ KGRFACSSIK TEGEIRSLLN LFRASLVAFP NEKVMEEAEI FSTTYLKEAV
     QKIPVSSLSR QIEYNMEYGW HTNLPRLEAR NYMGDMIHEM PYMNAEKLLE LAKLEFNIFH
     SLQERELKHL SRWWKDSGFS QLTFVRHRHV EYYTLASCID IDPKHSAFRL GFAKMCHLIT
     VLDDIYDTFG TMDELKLFTA AIKRWDPSAT EWLPEYMKGV YMVVYETVNE MAGEAKKSQG
     RDTINYSRQA WEAYIDSYMK EAEWISSGCL PTFEEYYENG KVSFGYQISV LQPILTLDVP
     LPHHILQEII FPSRFNGLAS GILRLKGDTR CYQADRARGE EASCISCYMN DNPGATEEDA
     LNHINAMVNE LMKEFNWELL KPDNNVPVSS KKHAFDITRV VHHGYKYRDG YSVANNEIKN
     LVITTVLEPV PL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025