GBIS2_ARATH
ID GBIS2_ARATH Reviewed; 554 AA.
AC Q9T0K1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=(Z)-gamma-bisabolene synthase 2;
DE EC=4.2.3.40;
DE AltName: Full=Terpenoid synthase 13;
DE Short=AtTPS13;
GN Name=TPS13; OrderedLocusNames=At4g13300; ORFNames=T9E8.40;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16297850; DOI=10.1016/j.abb.2005.09.019;
RA Ro D.-K., Ehlting J., Keeling C.I., Lin R., Mattheus N., Bohlmann J.;
RT "Microarray expression profiling and functional characterization of AtTPS
RT genes: duplicated Arabidopsis thaliana sesquiterpene synthase genes
RT At4g13280 and At4g13300 encode root-specific and wound-inducible (Z)-gamma-
RT bisabolene synthases.";
RL Arch. Biochem. Biophys. 448:104-116(2006).
CC -!- FUNCTION: Involved in sesquiterpene (C15) biosynthesis. The major
CC product is (Z)-gamma-bisabolene with minor amounts of (E)-nerolidol and
CC alpha-bisabolol. {ECO:0000269|PubMed:16297850}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (Z)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:26081, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49238, ChEBI:CHEBI:175763; EC=4.2.3.40;
CC Evidence={ECO:0000269|PubMed:16297850};
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: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots. Expressed in the
CC cortex and the sub-epidermal layers of roots. Also detected in leaf
CC hydathodes and flower stigmata. {ECO:0000269|PubMed:12566586,
CC ECO:0000269|PubMed:16297850}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:16297850}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40765.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78372.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049608; CAB40765.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161536; CAB78372.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83260.1; -; Genomic_DNA.
DR PIR; T06287; T06287.
DR RefSeq; NP_193066.4; NM_117403.5.
DR AlphaFoldDB; Q9T0K1; -.
DR SMR; Q9T0K1; -.
DR STRING; 3702.AT4G13300.1; -.
DR PaxDb; Q9T0K1; -.
DR PRIDE; Q9T0K1; -.
DR ProteomicsDB; 248560; -.
DR EnsemblPlants; AT4G13300.1; AT4G13300.1; AT4G13300.
DR GeneID; 826960; -.
DR Gramene; AT4G13300.1; AT4G13300.1; AT4G13300.
DR KEGG; ath:AT4G13300; -.
DR Araport; AT4G13300; -.
DR TAIR; locus:2142065; AT4G13300.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q9T0K1; -.
DR OMA; KEYCATE; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q9T0K1; -.
DR BioCyc; ARA:AT4G13300-MON; -.
DR BioCyc; MetaCyc:AT4G13300-MON; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9T0K1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0K1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052683; F:(Z)-gamma-bisabolene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009975; F:cyclase activity; IDA:TAIR.
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:0045338; P:farnesyl diphosphate metabolic process; IDA:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IBA:GO_Central.
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; 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 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..554
FT /note="(Z)-gamma-bisabolene synthase 2"
FT /id="PRO_0000380672"
FT MOTIF 306..310
FT /note="DDXXD motif"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 554 AA; 64145 MW; 2CF9322D5519FF98 CRC64;
MESQTKFDYE SLAFTKLSHS QWTDYFLSVP IDDSELDAIT REIDIIKPEV RKLLSSKGDD
ETSKRKVLLI QSLLSLGLAF HFENEIKDIL EDAFRRIDDI TGDENDLSTI SIMFRVFRTY
GHNLPSSVFK RFTGDDGKFE RSLTEDAKGI LSLYEAAHLG TTTDYILDEA LEFTSSHLKS
LLVGGMCRPH ILRLIRNTLY LPQRWNMEAV IAREYISFYE QEEDHDKMLL RLAKLNFKLL
QLHYIKELKT FIKWWMELGL TSKWPSQFRE RIVEAWLAGL MMYFEPQFSG GRVIAAKFNY
LLTILDDACD HYFSIPELTR LVDCVERWNH DGIHTLEDIS RIIFKLALDV FDDIGRGVRS
KGCSYYLKEM LEELKILVRA NLDLVKWARG NQLPSFEEHV EVGGIALTTY ATLMYSFVGM
GEAVGKEAYE WVRSRPRLIK SLAAKGRLMD DITDFESDMS NGFAANAINY YMKQFVVTKE
EAILECQKMV VDINKIVNEE LLKTTTVPRR VLKQALNFGR LLEVLYTKSD DIYNCSEGKL
KEYIVTLLID PIHL
