BARS_ARATH
ID BARS_ARATH Reviewed; 557 AA.
AC Q4KSH9; A3KPF7; Q9LU03;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alpha-barbatene synthase;
DE Short=AtBS;
DE EC=4.2.3.69;
DE AltName: Full=Beta-chamigrene synthase;
DE EC=4.2.3.78;
DE AltName: Full=Terpeneoid synthase 11;
DE Short=AtTPS11;
DE AltName: Full=Thujopsene synthase;
DE EC=4.2.3.79;
GN Name=BS; Synonyms=TPS11; OrderedLocusNames=At5g44630; ORFNames=K15C23.7;
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], AND FUNCTION.
RX PubMed=15965019; DOI=10.1104/pp.105.059386;
RA Wu S., Schoenbeck M.A., Greenhagen B.T., Takahashi S., Lee S., Coates R.M.,
RA Chappell J.;
RT "Surrogate splicing for functional analysis of sesquiterpene synthase
RT genes.";
RL Plant Physiol. 138:1322-1333(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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 Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2007) 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 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 [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15918888; DOI=10.1111/j.1365-313x.2005.02417.x;
RA Tholl D., Chen F., Petri J., Gershenzon J., Pichersky E.;
RT "Two sesquiterpene synthases are responsible for the complex mixture of
RT sesquiterpenes emitted from Arabidopsis flowers.";
RL Plant J. 42:757-771(2005).
CC -!- FUNCTION: Involved in the biosynthesis of over 15 sesquiterpenes (C15).
CC The major products are (+)-alpha-barbatene (27.3%), (+)-thujopsene
CC (17.8%) and (+)-beta-chamigrene (9.9%). Can use farnesyl diphosphate or
CC geranyl diphosphate as substrates, but not geranylgeranyl diphosphate.
CC {ECO:0000269|PubMed:15918888, ECO:0000269|PubMed:15965019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-alpha-barbatene +
CC diphosphate; Xref=Rhea:RHEA:29499, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61690, ChEBI:CHEBI:175763; EC=4.2.3.69;
CC Evidence={ECO:0000269|PubMed:15918888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-thujopsene + diphosphate;
CC Xref=Rhea:RHEA:30375, ChEBI:CHEBI:33019, ChEBI:CHEBI:61737,
CC ChEBI:CHEBI:175763; EC=4.2.3.79;
CC Evidence={ECO:0000269|PubMed:15918888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-beta-chamigrene +
CC diphosphate; Xref=Rhea:RHEA:30379, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61746, ChEBI:CHEBI:175763; EC=4.2.3.78;
CC Evidence={ECO:0000269|PubMed:15918888};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for farnesyl diphosphate {ECO:0000269|PubMed:15918888};
CC KM=0.21 uM for geranyl diphosphate {ECO:0000269|PubMed:15918888};
CC Note=The formation of monoterpene products from geranyl diphosphate
CC (GPP) is unlikely, as the protein is not expected to be present in
CC plastids, where GPP is thought to be produced.;
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in flowers. Expressed in
CC intrafloral nectaries and in the funiculus within the ovules.
CC {ECO:0000269|PubMed:12566586, ECO:0000269|PubMed:15918888}.
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: Does not emit any sesquiterpene volatiles except
CC (E)-beta-caryophyllene, alpha-copaene and alpha-humulene.
CC {ECO:0000269|PubMed:15918888}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY876386; AAX59990.1; -; mRNA.
DR EMBL; AB024024; BAA98116.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95140.1; -; Genomic_DNA.
DR EMBL; BT030324; ABO09887.1; -; mRNA.
DR RefSeq; NP_199276.1; NM_123830.3.
DR AlphaFoldDB; Q4KSH9; -.
DR SMR; Q4KSH9; -.
DR STRING; 3702.AT5G44630.1; -.
DR iPTMnet; Q4KSH9; -.
DR PaxDb; Q4KSH9; -.
DR PRIDE; Q4KSH9; -.
DR ProteomicsDB; 240741; -.
DR EnsemblPlants; AT5G44630.1; AT5G44630.1; AT5G44630.
DR GeneID; 834491; -.
DR Gramene; AT5G44630.1; AT5G44630.1; AT5G44630.
DR KEGG; ath:AT5G44630; -.
DR Araport; AT5G44630; -.
DR TAIR; locus:2152155; AT5G44630.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q4KSH9; -.
DR OMA; YMENLHG; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q4KSH9; -.
DR BioCyc; ARA:AT5G44630-MON; -.
DR BioCyc; MetaCyc:AT5G44630-MON; -.
DR BRENDA; 4.2.3.69; 399.
DR BRENDA; 4.2.3.78; 399.
DR BRENDA; 4.2.3.79; 399.
DR SABIO-RK; Q4KSH9; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q4KSH9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q4KSH9; baseline and differential.
DR Genevisible; Q4KSH9; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0102878; F:(+)-alpha-barbatene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102883; F:(+)-beta-chamigrene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102879; F:(+)-thujopsene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009975; F:cyclase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:TAIR.
DR GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IDA:TAIR.
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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..557
FT /note="Alpha-barbatene synthase"
FT /id="PRO_0000380673"
FT MOTIF 310..314
FT /note="DDXXD motif"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 162
FT /note="F -> Y (in Ref. 1; AAX59990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 64909 MW; 05439A5144A37240 CRC64;
MEALGNFDYE SYTNFTKLPS SQWGDQFLKF SIADSDFDVL EREIEVLKPK VRENIFVSSS
TDKDAMKKTI LSIHFLDSLG LSYHFEKEIE ESLKHAFEKI EDLIADENKL HTISTIFRVF
RTYGYYMSSD VFKIFKGDDG KFKESLIEDV KGMLSFYEAV HFGTTTDHIL DEALSFTLNH
LESLATGRRA SPPHISKLIQ NALHIPQHRN IQALVAREYI SFYEHEEDHD ETLLKLAKLN
FKFLQLHYFQ ELKTITMWWT KLDHTSNLPP NFRERTVETW FAALMMYFEP QFSLGRIMSA
KLYLVITFLD DACDTYGSIS EVESLADCLE RWDPDYMENL QGHMKTAFKF VMYLFKEYEE
ILRSQGRSFV LEKMIEEFKI IARKNLELVK WARGGHVPSF DEYIESGGAE IGTYATIACS
IMGLGEIGKK EAFEWLISRP KLVRILGAKT RLMDDIADFE EDMEKGYTAN ALNYYMNEHG
VTKEEASREL EKMNGDMNKI VNEECLKITT MPRRILMQSV NYARSLDVLY TADDVYNHRE
GKLKEYMRLL LVDPILL
