TPSD2_ABIGR
ID TPSD2_ABIGR Reviewed; 627 AA.
AC O24474;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Myrcene synthase, chloroplastic;
DE EC=4.2.3.15;
DE AltName: Full=Aggmyr;
DE Flags: Precursor;
GN Name=ag2; Synonyms=AG2.2;
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], INDUCTION, AND CHARACTERIZATION.
RX PubMed=9268308; DOI=10.1074/jbc.272.35.21784;
RA Bohlmann J., Steele C.L., Croteau R.B.;
RT "Monoterpene synthases from grand fir (Abies grandis). cDNA isolation,
RT characterization, and functional expression of myrcene synthase, (-)-(4S)-
RT limonene synthase, and (-)-(1S,5S)-pinene synthase.";
RL J. Biol. Chem. 272:21784-21792(1997).
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:11404343,
CC ECO:0000269|PubMed:9539701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
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;
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:9268308}.
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 64-Arg-Arg-65 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; U87908; AAB71084.1; -; mRNA.
DR AlphaFoldDB; O24474; -.
DR SMR; O24474; -.
DR KEGG; ag:AAB71084; -.
DR BioCyc; MetaCyc:MON-12818; -.
DR BRENDA; 4.2.3.15; 2.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
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; Plastid;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..627
FT /note="Myrcene synthase, chloroplastic"
FT /id="PRO_0000033627"
FT MOTIF 378..382
FT /note="DDXXD motif"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 627 AA; 72479 MW; 2E0DA492E0C971FD CRC64;
MALVSISPLA SKSCLRKSLI SSIHEHKPPY RTIPNLGMRR RGKSVTPSMS ISLATAAPDD
GVQRRIGDYH SNIWDDDFIQ SLSTPYGEPS YQERAERLIV EVKKIFNSMY LDDGRLMSSF
NDLMQRLWIV DSVERLGIAR HFKNEITSAL DYVFRYWEEN GIGCGRDSIV TDLNSTALGF
RTLRLHGYTV SPEVLKAFQD QNGQFVCSPG QTEGEIRSVL NLYRASLIAF PGEKVMEEAE
IFSTRYLKEA LQKIPVSALS QEIKFVMEYG WHTNLPRLEA RNYIDTLEKD TSAWLNKNAG
KKLLELAKLE FNIFNSLQQK ELQYLLRWWK ESDLPKLTFA RHRHVEFYTL ASCIAIDPKH
SAFRLGFAKM CHLVTVLDDI YDTFGTIDEL ELFTSAIKRW NSSEIEHLPE YMKCVYMVVF
ETVNELTREA EKTQGRNTLN YVRKAWEAYF DSYMEEAKWI SNGYLPMFEE YHENGKVSSA
YRVATLQPIL TLNAWLPDYI LKGIDFPSRF NDLASSFLRL RGDTRCYKAD RDRGEEASCI
SCYMKDNPGS TEEDALNHIN AMVNDIIKEL NWELLRSNDN IPMLAKKHAF DITRALHHLY
IYRDGFSVAN KETKKLVMET LLESMLF
