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TPS1B_CAMHI
ID   TPS1B_CAMHI             Reviewed;         554 AA.
AC   A0A348AUV6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Valerianol synthase TPS1B {ECO:0000305};
DE            EC=4.2.3.204 {ECO:0000269|PubMed:30127518};
DE   AltName: Full=Terpene synthase 1b {ECO:0000303|PubMed:30127518};
DE            Short=ChTps1b {ECO:0000303|PubMed:30127518};
GN   Name=TPS1B {ECO:0000303|PubMed:30127518};
OS   Camellia hiemalis (Camellia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Theaceae; Camellia.
OX   NCBI_TaxID=1840584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=30127518; DOI=10.1038/s41598-018-30653-w;
RA   Hattan J., Shindo K., Sasaki T., Ohno F., Tokuda H., Ishikawa K.,
RA   Misawa N.;
RT   "Identification of novel sesquiterpene synthase genes that mediate the
RT   biosynthesis of valerianol, which was an unknown ingredient of tea.";
RL   Sci. Rep. 8:12474-12474(2018).
CC   -!- FUNCTION: Terpene synthase that catalyzes the biosynthesis of the
CC       terpene valerianol, which is a volatile compound of floral scent.
CC       {ECO:0000269|PubMed:30127518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + valerianol;
CC         Xref=Rhea:RHEA:60424, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:143779, ChEBI:CHEBI:175763; EC=4.2.3.204;
CC         Evidence={ECO:0000269|PubMed:30127518};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60425;
CC         Evidence={ECO:0000269|PubMed:30127518};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305}.
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. {ECO:0000305}.
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DR   EMBL; LC212977; BBC44637.1; -; mRNA.
DR   AlphaFoldDB; A0A348AUV6; -.
DR   SMR; A0A348AUV6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; 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: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   2: Evidence at transcript level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..554
FT                   /note="Valerianol synthase TPS1B"
FT                   /id="PRO_0000451720"
FT   MOTIF           326..330
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   554 AA;  64163 MW;  F7A16E214F9476D1 CRC64;
     MASSQVGDMV NGNAEPTRHL AKFPPSLWGD RFTSFTLDKQ LWDKYGNEIE VLKEQVRSMV
     VAGGRKAAEQ INLINVLQRL GVSYHFEKEI EEQLEQLFAK FEDNEDYDLF TIALHFRIFR
     QHGYKMSCDV FNKFRDSNGE FKETMSNDVQ GMLSLYEATY LKIRGEGFLD EAHAFTIAQL
     ESLVEGPHLS SDLSEQVMHA LKQSIHRGFP RLEAKHFISF YEKDASRNET LLRLAKLDFN
     QLQLSHREEL CHIFRWWKEL DLISKVPYAR DRAVECFFWS TCAYYEPQHS VGRAVLTKIM
     LLLSVTDDTY DAYGTYNELK IYTNAVQRWD VSAMDELPDY MKALYRALLN VYDEVERDLA
     KQGRAYGVHH SKEAFKEIVR SYEIEAEWFK EGYVASFEEY MKNALVTSTG RLHTTSCFMG
     LEADVATTEA FEWILTKPKM VAASGAIGRL VDDVMSHDEE QERGHVATGL DCYMKQHGVS
     KQEAIVELYK MIENAWRDIN EEMLKPTAIS MKLLIRVLNL SRISDVVYKY VDGYTHPEII
     KDHVISLFED PIPM
 
 
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