ID MYRS2_ARATH Reviewed; 598 AA.
AC Q9LRZ6; B7ZWS1; Q84UV1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Beta-myrcene/(E)-beta-ocimene synthase 2, chloroplastic;
DE EC=4.2.3.15 {ECO:0000269|PubMed:12566586};
DE AltName: Full=Terpenoid synthase 24;
DE Short=AtTPS24;
DE Flags: Precursor;
GN Name=TPS24; OrderedLocusNames=At3g25810 {ECO:0000312|Araport:AT3G25810};
GN ORFNames=K13N2.7 {ECO:0000312|EMBL:BAA95770.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12566586; DOI=10.1105/tpc.007989;
RA Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT flowers.";
RL Plant Cell 15:481-494(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA Aubourg S., Lecharny A., Bohlmann J.;
RT "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 267:730-745(2002).
RN [6]
RP GENE FAMILY.
RX PubMed=12777052; DOI=10.1023/a:1023005504702;
RA Lange B.M., Ghassemian M.;
RT "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT in isoprenoid and chlorophyll metabolism.";
RL Plant Mol. Biol. 51:925-948(2003).
CC -!- FUNCTION: Involved in monoterpene (C10) biosynthesis. The major
CC products are alpha- and beta-pinene, sabinene, beta-myrcene, (E)-beta-
CC ocimene and limonene. {ECO:0000269|PubMed:12566586}.
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 Evidence={ECO:0000269|PubMed:12566586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=1.7 pmol/sec/mg enzyme toward geranyl diphosphate
CC {ECO:0000269|PubMed:12566586};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:12566586}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in mature flowers, but not in
CC inmmature buds. {ECO:0000269|PubMed:12566586}.
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:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AF497484; AAO85532.1; -; mRNA.
DR EMBL; AB028607; BAA95770.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77072.1; -; Genomic_DNA.
DR EMBL; BT053763; ACL13990.1; -; mRNA.
DR RefSeq; NP_189209.2; NM_113482.5.
DR AlphaFoldDB; Q9LRZ6; -.
DR SMR; Q9LRZ6; -.
DR BioGRID; 7504; 1.
DR IntAct; Q9LRZ6; 1.
DR STRING; 3702.Q9LRZ6; -.
DR PaxDb; 3702-AT3G25810-1; -.
DR ProteomicsDB; 251358; -.
DR EnsemblPlants; AT3G25810.1; AT3G25810.1; AT3G25810.
DR GeneID; 822173; -.
DR Gramene; AT3G25810.1; AT3G25810.1; AT3G25810.
DR KEGG; ath:AT3G25810; -.
DR Araport; AT3G25810; -.
DR TAIR; AT3G25810; -.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR InParanoid; Q9LRZ6; -.
DR OMA; HAFNISR; -.
DR OrthoDB; 1212461at2759; -.
DR PhylomeDB; Q9LRZ6; -.
DR BioCyc; ARA:AT3G25810-MONOMER; -.
DR BioCyc; MetaCyc:AT3G25810-MONOMER; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9LRZ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRZ6; baseline and differential.
DR Genevisible; Q9LRZ6; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IDA:TAIR.
DR GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:TAIR.
DR GO; GO:0034002; F:(R)-limonene synthase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IDA:TAIR.
DR GO; GO:0050550; F:pinene synthase activity; IDA:TAIR.
DR GO; GO:0080015; F:sabinene synthase activity; IDA:TAIR.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:TAIR.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IDA:TAIR.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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 PANTHER; PTHR31225:SF9; 1,8-CINEOLE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..598
FT /note="Beta-myrcene/(E)-beta-ocimene synthase 2,
FT chloroplastic"
FT /id="PRO_0000348418"
FT MOTIF 344..348
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 344
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 348
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 486
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 489
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 32
FT /note="S -> A (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="M -> I (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="N -> Y (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="I -> T (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="G -> D (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="A -> V (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="S -> I (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="R -> G (in Ref. 2; AAO85532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 69812 MW; 8BC02555898C5C60 CRC64;
MATLCIGSAP IYQNACIHNF RLQRPRRFIS KSMTKTMPDA NPLDLRRRSG NYQPSSWDHS
YLLSIENKYV NEKEVITRHV LKKKVKKMLE EVETKSRLEK LELIDDLQKL GVSYHFEQEI
NNILTNFHLE NGKNIWKCDK EEDLHATALE FRLLRQHGFG VSEDIFDVII DKIESNTFKS
DNITSIITLY EASYLSTKSD TKLHKVIRPF ATEQIRNFVD DESETYNIML REMAIHALEI
PYHWRMRRLE TRWYIDAYEK KHDMNLFLAE FAKIDFNIVQ TAHQEDVKYV SCWWKETGLG
SQLHFVRDRI VENYFWTVGM IYEPQFGYIR RIVAIVAALI TVIDDIYDIY GTPEELELFT
AMVQNWDINR LDELPEYMKL CFLTLFNEIN AMGCDVLKCK NIDVIPYFKK SWADLCKAYL
VEAKWYKGGY KPSVEEYMQN AWISISAPTM LIHFYCAFSG QISVQILESL VQQQQDVVRC
SATVLRLAND LATSPDELAR GDVLKSVQCY MHETGVSEEE ARTHVQQMIS HTWDEMNYEA
RTAARSSSLL SRRFVETAMN LARMSQCMYQ HGDGHGCPDK AKIVDRVQTL LVDPIPLD
//
