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TPSDB_ABIGR
ID   TPSDB_ABIGR             Reviewed;         637 AA.
AC   Q9M7C9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Limonene/alpha-pinene synthase, chloroplastic;
DE   AltName: Full=(-)-(1S,5S)-alpha-pinene synthase;
DE            EC=4.2.3.119;
DE   AltName: Full=(-)-(4S)-limonene synthase;
DE            EC=4.2.3.16;
DE   AltName: Full=Agg-pin2;
DE   Flags: Precursor;
GN   Name=ag11; Synonyms=agc11;
OS   Abies grandis (Grand fir) (Pinus grandis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX   NCBI_TaxID=46611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Stem;
RX   PubMed=10441373; DOI=10.1006/abbi.1999.1332;
RA   Bohlmann J., Phillips M., Ramachandiran V., Katoh S., Croteau R.B.;
RT   "cDNA cloning, characterization, and functional expression of four new
RT   monoterpene synthase members of the Tpsd gene family from grand fir (Abies
RT   grandis).";
RL   Arch. Biochem. Biophys. 368:232-243(1999).
RN   [2]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=9539701; DOI=10.1073/pnas.95.8.4126;
RA   Bohlmann J., Meyer-Gauen G., Croteau R.B.;
RT   "Plant terpenoid synthases: molecular biology and phylogenetic analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
RN   [3]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA   Trapp S.C., Croteau R.B.;
RT   "Genomic organization of plant terpene synthases and molecular evolutionary
RT   implications.";
RL   Genetics 158:811-832(2001).
CC   -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC       response to insect attack or other injury. Involved in monoterpene
CC       (C10) olefins biosynthesis. {ECO:0000269|PubMed:10441373,
CC       ECO:0000269|PubMed:11404343, ECO:0000269|PubMed:9539701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC         Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.16;
CC         Evidence={ECO:0000269|PubMed:10441373};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate;
CC         Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.119;
CC         Evidence={ECO:0000269|PubMed:10441373};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal part of the protein seems to be involved in the
CC       cyclization step(s) required for the synthesis of pinene.
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   -!- MISCELLANEOUS: The conserved 70-Arg-Arg-71 motif may play a role in the
CC       isomerization step of the terpenoid cyclization reaction sequence.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF139207; AAF61455.1; -; mRNA.
DR   AlphaFoldDB; Q9M7C9; -.
DR   SMR; Q9M7C9; -.
DR   KEGG; ag:AAF61455; -.
DR   BioCyc; MetaCyc:AG11-MON; -.
DR   BRENDA; 4.2.3.119; 2.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050552; F:(4S)-limonene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; 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   Chloroplast; Lyase; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Plastid; Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..637
FT                   /note="Limonene/alpha-pinene synthase, chloroplastic"
FT                   /id="PRO_0000033633"
FT   MOTIF           388..392
FT                   /note="DDXXD motif"
FT   BINDING         388
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         540
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   637 AA;  73273 MW;  B3574986FEC96CFB CRC64;
     MALLSIVSLQ VPKSCGLKSL ISSSNVQKAL CISTAVPTLR MRRRQKALVI NMKLTTVSHR
     DDNGGGVLQR RIADHHPNLW EDDFIQSLSS PYGGSSYSER AVTVVEEVKE MFNSIPNNRE
     LFGSQNDLLT RLWMVDSIER LGIDRHFQNE IRVALDYVYS YWKEKEGIGC GRDSTFPDLN
     STALALRTLR LHGYNVSSDV LEYFKDQKGH FACPAILTEG QITRSVLNLY RASLVAFPGE
     KVMEEAEIFS ASYLKEVLQK IPVSSFSREI EYVLEYGWHT NLPRLEARNY IDVYGQDSYE
     SSNEMPYVNT QKLLKLAKLE FNIFHSLQQK ELQYISRWWK DSCSSHLTFT RHRHVEYYTM
     ASCISMEPKH SAFRLGFVKT CHLLTVLDDM YDTFGTLDEL QLFTTAFKRW DLSETKCLPE
     YMKAVYMDLY QCLNELAQEA EKTQGRDTLN YIRNAYESHF DSFMHEAKWI SSGYLPTFEE
     YLKNGKVSSG SRTATLQPIL TLDVPLPNYI LQEIDYPSRF NDLASSLLRL RGDTRCYKAD
     RARGEEASAI SCYMKDHPGS TEEDALNHIN VMISDAIREL NWELLRPDSK SPISSKKHAF
     DITRAFHHLY KYRDGYTVAS SETKNLVMKT VLEPVAL
 
 
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