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BCPSD_ORIVU
ID   BCPSD_ORIVU             Reviewed;         554 AA.
AC   E2E2N5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=(E)-beta-caryophyllene synthase {ECO:0000305|PubMed:20419468};
DE            EC=4.2.3.57 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE   AltName: Full=Alpha-humulene synthase {ECO:0000305|PubMed:20419468};
DE            EC=4.2.3.104 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE   AltName: Full=Terpene synthase 6 {ECO:0000303|PubMed:20419468};
DE            Short=OvTPS6 {ECO:0000303|PubMed:20419468};
GN   Name=TPS6 {ECO:0000303|PubMed:20419468};
OS   Origanum vulgare (Wild marjoram).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Origanum.
OX   NCBI_TaxID=39352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. d06-01; TISSUE=Trichome gland;
RX   PubMed=20419468; DOI=10.1007/s11103-010-9636-1;
RA   Crocoll C., Asbach J., Novak J., Gershenzon J., Degenhardt J.;
RT   "Terpene synthases of oregano (Origanum vulgare L.) and their roles in the
RT   pathway and regulation of terpene biosynthesis.";
RL   Plant Mol. Biol. 73:587-603(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RA   Crocoll C.;
RT   "Biosynthesis of the phenolic monoterpenes, thymol and carvacrol, by
RT   terpene synthases and cytochrome P450s in oregano and thyme.";
RL   Thesis (2011), Friedrich Schiller University of Jena, Germany.
RN   [3]
RP   TISSUE SPECIFICITY.
RX   DOI=10.1016/j.indcrop.2018.07.006;
RA   Jan S., Mir J.I., Shafi W., Faktoo S.Z., Singh D.B., Wijaya L.,
RA   Alyemeni M.N., Ahmad P.;
RT   "Divergence in tissue-specific expression patterns of genes associated with
RT   the terpenoid biosynthesis in two oregano species Origanum vulgare L., and
RT   Origanum majorana.";
RL   Ind. Crops Prod. 123:546-555(2018).
CC   -!- FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes
CC       natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-
CC       farnesyl diphosphate (FPP) to (E)-beta-caryophyllene and alpha-humulene
CC       (PubMed:20419468, Ref.2). {ECO:0000269|PubMed:20419468,
CC       ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC         diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC         Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:175763; EC=4.2.3.104;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
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:20419468, ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0M3Q1Q3}.
CC   -!- TISSUE SPECIFICITY: Expressed in peltate glandular trichomes
CC       (PubMed:20419468). Present at low levels in flowers, leaves and stems
CC       (Ref.3). {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.3}.
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; GU385970; ADK73616.1; -; mRNA.
DR   SMR; E2E2N5; -.
DR   UniPathway; UPA00213; -.
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   Lyase; Manganese; Metal-binding.
FT   CHAIN           1..554
FT                   /note="(E)-beta-caryophyllene synthase"
FT                   /id="PRO_0000453320"
FT   REGION          319..325
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT   REGION          391..427
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT   MOTIF           313..317
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X839"
FT   BINDING         313
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         313
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         317
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         317
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         457
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         465
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ   SEQUENCE   554 AA;  64724 MW;  FDDDA6A9D71C4344 CRC64;
     MEFPASVASL SANTVGSNDV LRRSIAYHPN IWGDFFLAHT SEFMEISIAE KEEHERLKEE
     IKKLLVQTEY DSILKLELID SIQRLGVGYH FEKEIDRILR YVHQTYPIYD TENKDLRMLA
     LRFRLLRQQG FHVPFDVLSE FIDAEGNLTE SIAYDIQGIL SLYEASNYGV LGEEILDKAL
     DSCSSRLESL ITDTDDDRLS RQVKEALKIP ISKTLTRLGA RKFISMYKED DSHNEKLLKF
     AMLDFNMVQR LHQNELSHLT RWWKELDFAN KLPFARDRLV ECYFWIMGVY YEPRHEIARK
     ILTKVIYMAS VLDDIYDVYG TLDELTLFTS FVRRWDISGI DELPTYMRIY LRALFDVYVE
     MEEEMGKIGK SYAIEYAKEE MKRLAEVYFQ EAQWFFSKYK PTMQEYMKVA LLSSGYMMMT
     INSLAVIKDP ITKKEFDWVV SEPPILKSSS IITRLMDDLA GYGSEEKHSA VHLYMNEKGV
     SEEEAFQELR KQVKNSWKNI NKECLKLRPA SVPILTTVVN FTRVIIVLYT DEDAYGNSKT
     KTKDMIKSIL VDPV
 
 
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