OCISB_ARATH
ID OCISB_ARATH Reviewed; 589 AA.
AC P0CJ43; O23516;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=(E)-beta-ocimene synthase, chloroplastic;
DE EC=4.2.3.-;
DE AltName: Full=(E,E)-alpha-farnesene synthase;
DE EC=4.2.3.46;
DE AltName: Full=Terpenoid synthase 2;
DE Short=AtTPS02;
DE Flags: Precursor;
GN Name=TPS02;
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 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 [2]
RP TISSUE SPECIFICITY.
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 [3]
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).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=20463089; DOI=10.1104/pp.110.154864;
RA Huang M., Abel C., Sohrabi R., Petri J., Haupt I., Cosimano J.,
RA Gershenzon J., Tholl D.;
RT "Variation of herbivore-induced volatile terpenes among Arabidopsis
RT ecotypes depends on allelic differences and subcellular targeting of two
RT terpene synthases, TPS02 and TPS03.";
RL Plant Physiol. 153:1293-1310(2010).
CC -!- FUNCTION: Predominantly involved in monoterpene (C10) biosynthesis.
CC Using GPP as substrate, the major product is (E)-beta-ocimene with
CC minor amounts of (Z)-beta-ocimene and myrcene. Using FPP as substrate,
CC could also be able to synthesize in vitro sesquiterpenes (C15) with
CC (E,E)-alpha-farnesene as the major product and with (Z,E)-alpha-
CC farnesene and (E,E)-beta-farnesene as minor products.
CC {ECO:0000269|PubMed:20463089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20463089}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in flowers.
CC {ECO:0000269|PubMed:12566586}.
CC -!- INDUCTION: By coronalon. Also induced in response to the caterpillar
CC P.xylostella feeding. {ECO:0000269|PubMed:20463089}.
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 -!- DISRUPTION PHENOTYPE: No formation of (E)-beta-ocimene detected.
CC {ECO:0000269|PubMed:20463089}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Has been shown to be a pseudogene in cv. Columbia (AC P0CJ42)
CC due to a naturally occurring frameshift at position 65 in this strain.
CC The sequence shown is from strain cv. Wassilewskija. {ECO:0000305}.
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DR AlphaFoldDB; P0CJ43; -.
DR SMR; P0CJ43; -.
DR STRING; 3702.AT4G16730.1; -.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR PhylomeDB; P0CJ43; -.
DR BRENDA; 4.2.3.46; 399.
DR UniPathway; UPA00213; -.
DR ExpressionAtlas; P0CJ43; baseline and differential.
DR Genevisible; P0CJ43; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052578; F:alpha-farnesene synthase activity; IEA:RHEA.
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 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 26..589
FT /note="(E)-beta-ocimene synthase, chloroplastic"
FT /id="PRO_0000403699"
FT MOTIF 339..343
FT /note="DDXXD motif"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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"
SQ SEQUENCE 589 AA; 69047 MW; E0243F0230827EE6 CRC64;
MAAHNLCFNS AFVCNVHHQK TQHFPCNAVS KTTSTHAVTF HRRSANYRPP LWDHQYLLSL
ENIYVKEVET AEKAILFKEE VRKTLNEIEG SIEQLEMIDS LQRLGISYHY KHEIHDILRK
IHDQHGEIER ETQDLHATSL EFILLRQHGF DVSQDAFDVF ISETGEFRKT LHSDIKGLLS
LYEASYFSMD SEFKLKETRI YANKRLSEFV AESSKTICRE DETYILEMVK RALETPYHWS
IRRLEARWYI NVYEKKHEMN PLLLEFAAID FNMLQANHQE ELKLISSWWN STGLMKQLDF
VRDRITESYF WTIGIFYEPE FKYCRKILTK IFMLIVIMDD IYDIYGTLEE LELFTNVVEK
WDVNHVERLP NYMRMCFLFL YNEINQIGYD VLRDKGLNVI PYLKQVWTDL FKTFLTESKW
YKTGHKPSFE EYMQNGVISS SVPTILLHLF SVLSDHISDQ TLTDDSKNHS VVRSCATILR
LANDLATSTE EMARGDSPKS VQCYMYETRA SEEEARRHMQ SMISDSWDII NSDLKTAHTS
SLPRGFLAAA ANLNRVVQCI YRHGDGHGSP EKTKTVDYIQ SVLFNPVPL
