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ATESY_MAGGA
ID   ATESY_MAGGA             Reviewed;         592 AA.
AC   B3TPQ7;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Alpha-terpineol synthase, chloroplastic;
DE            Short=Mg17;
DE            EC=4.2.3.111;
DE            EC=4.2.3.112;
DE   Flags: Precursor;
OS   Magnolia grandiflora (Southern magnolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Magnoliaceae;
OC   Magnolia.
OX   NCBI_TaxID=3406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=18467455; DOI=10.1104/pp.108.115824;
RA   Lee S., Chappell J.;
RT   "Biochemical and genomic characterization of terpene synthases in Magnolia
RT   grandiflora.";
RL   Plant Physiol. 147:1017-1033(2008).
CC   -!- FUNCTION: Monoterpene synthase converting geranyl diphosphate into
CC       alpha-terpineol. In vitro, can also have an sesquiterpene synthase
CC       activity, converting farnesyl diphosphate into (E)-alpha-bisabolene
CC       (33.1%), alpha-bisabolene (18.7%), beta-sesquiphellandrene (15.8%),
CC       beta-bergamotene (12.6%), (Z)-alpha-farnesene (10.4%), and (Z)-alpha-
CC       bisabolene (9.4%). {ECO:0000269|PubMed:18467455}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol +
CC         diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC         EC=4.2.3.111; Evidence={ECO:0000269|PubMed:18467455};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + H2O = (R)-alpha-terpineol +
CC         diphosphate; Xref=Rhea:RHEA:32555, ChEBI:CHEBI:300,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC         EC=4.2.3.112; Evidence={ECO:0000269|PubMed:18467455};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000305|PubMed:18467455}. Note=The transit peptide can target GFP
CC       to both chloroplasts and mitochondria when transiently expressed in a
CC       heterologous system.
CC   -!- TISSUE SPECIFICITY: Expressed in young developing leaves. Barely
CC       detected in tepals, carpels and stamens. {ECO:0000269|PubMed:18467455}.
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}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU366430; ACC66282.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3TPQ7; -.
DR   SMR; B3TPQ7; -.
DR   PRIDE; B3TPQ7; -.
DR   BioCyc; MetaCyc:MON-14948; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033383; P:geranyl diphosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0043693; P:monoterpene 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; 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   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..42
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..592
FT                   /note="Alpha-terpineol synthase, chloroplastic"
FT                   /id="PRO_0000419801"
FT   MOTIF           342..346
FT                   /note="DDXXD motif"
FT   BINDING         342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         487
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         495
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   592 AA;  67904 MW;  C73FB6E07B118729 CRC64;
     MALKLLFQCS PCSPSSLAPL QPVLVLVRPP SGAKARRNLR CCASTQVTEL MTARRSANYH
     PNIWDYDSVQ SLTSDYKAYT YLERVEKLKE DVRRTLQEAV GLLDQLELVD CIHRLGVGYH
     FDKEIKEILK TISTEPNNMG LIDGDLYAMA LYFRLLRQHG YEVPQGVFNR FMDDSSSFKA
     SLCNDVKGML SLYEASYLAL EGETTLDEAK AFTYRHLRGL KGNIDSNLKG LVEHALELPL
     HWRVLRLEAR WYIDTYERME DMNPLLLELA KLDFNIVQNV YQGQVRKMSG WWKDLGLGQK
     LGFARDRLME GFLWTIGVKF EPQFAQCREV LTKINQLITT IDDVYDVYGS LEELELFTKA
     VDRWDTNAME ELPEYMKICF LALYNTVNEI AYDTLKEQGV DVIPYLQKSW ADLCKAYLVE
     ARWYYSGYTP TLDEYLNNAW ISIAGPVILV HAYVSMIQMI TKEALLDCVG SYESIMQWSS
     MILRLADDLA TSTDELERGD VPKSIQCYMH ENTASEVVAR EQMRARISDI WKKMNKDVAL
     SPLPQPFKAA AVNLARMAQC MYQHGDGHGN PHRESKDHIL SLVVEPIQLM ES
 
 
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