TPS08_ARATH
ID TPS08_ARATH Reviewed; 600 AA.
AC O65435;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Terpenoid synthase 8;
DE Short=AtTPS08;
DE EC=4.2.3.195;
GN Name=TPS08; OrderedLocusNames=At4g20210; ORFNames=F1C12.130;
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23512856; DOI=10.1105/tpc.112.100057;
RA Vaughan M.M., Wang Q., Webster F.X., Kiemle D., Hong Y.J., Tantillo D.J.,
RA Coates R.M., Wray A.T., Askew W., O'Donnell C., Tokuhisa J.G., Tholl D.;
RT "Formation of the unusual semivolatile diterpene rhizathalene by the
RT Arabidopsis class I terpene synthase TPS08 in the root stele is involved in
RT defense against belowground herbivory.";
RL Plant Cell 25:1108-1125(2013).
CC -!- FUNCTION: Catalyzes the synthesis of the semivolatile diterpene
CC rhizatalene A. {ECO:0000269|PubMed:23512856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate +
CC rhizathalene A; Xref=Rhea:RHEA:55216, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:138656; EC=4.2.3.195;
CC Evidence={ECO:0000269|PubMed:23512856};
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=0.8 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:23512856};
CC Vmax=4.6 pmol/sec/mg enzyme {ECO:0000269|PubMed:23512856};
CC Note=kcat is 0.0003 sec(-1). {ECO:0000269|PubMed:23512856};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:23512856}.
CC -!- TISSUE SPECIFICITY: Stele, and tips of primary and secondary root.
CC {ECO:0000269|PubMed:23512856}.
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=CAA18246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79021.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022224; CAA18246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161552; CAB79021.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84285.1; -; Genomic_DNA.
DR PIR; T05329; T05329.
DR RefSeq; NP_193754.2; NM_118140.3.
DR AlphaFoldDB; O65435; -.
DR SMR; O65435; -.
DR STRING; 3702.AT4G20210.1; -.
DR PaxDb; O65435; -.
DR PRIDE; O65435; -.
DR ProteomicsDB; 232492; -.
DR EnsemblPlants; AT4G20210.1; AT4G20210.1; AT4G20210.
DR GeneID; 827768; -.
DR Gramene; AT4G20210.1; AT4G20210.1; AT4G20210.
DR KEGG; ath:AT4G20210; -.
DR Araport; AT4G20210; -.
DR TAIR; locus:2120337; AT4G20210.
DR eggNOG; ENOG502SHPY; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; O65435; -.
DR OMA; TEYIMEE; -.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.195; 399.
DR UniPathway; UPA00213; -.
DR PRO; PR:O65435; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65435; baseline and differential.
DR Genevisible; O65435; AT.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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 Lyase; Magnesium; Manganese; Metal-binding; Plastid; Reference proteome.
FT CHAIN 1..600
FT /note="Terpenoid synthase 8"
FT /id="PRO_0000403704"
FT MOTIF 352..356
FT /note="DDXXD motif"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 69095 MW; 2B7B5528B0C861DF CRC64;
MEAIKTFSPK FGFQISLSPR THLTPVRFPP TACPVKPANL VRLKATRALI RDPQESNRKF
QKFPPSEWTN RFDSVSVDAS EMDALRKEID KIIPNVKKEL MSSQGIESTK KKILMVYLLV
SLGLAYHFED EIEECLKEGF ETIEEMMAGE DNLYTISIIF LVLRTYGHHM SSDIFQKFKG
NDGNFKGCIS GDAKGLLALY EAAQLRTTTE YIMEEALSFT SSNLELLAAD GRCPPHLSKH
IRNALGLSQH KQMEVLVAVE YISFYEQEKD HDKILLKFAK LNFKLMQLHY LEELKVVTKW
YKEHDFASNL PPYFKYVIVE NHFFAITMYF EPKFSQKRIM LAKYFTVLVL LDDTCDRYAS
LSEAESLTNS LERWAPDDAM DKQPHYLKFV FKFIMGCFEE FERELASEGR SYSVKATLEE
FKTIVKANFD FAKLAHTGHV PSFKEYMEVG EVEVGVCATL AGNLMCIGHI GDEGVYEWLK
SRPKFLKAAS TYGRLMNDIA GFEDDMKREY VITGVNTYMK QYGLTKMEAI RELQNLVEYN
HTIMNEEFLK TTDLPRQIRK QVINVARSLN VSYTEGEGFT HTKGKVDEYI TSLFITPIRI
