TPS06_ARATH
ID TPS06_ARATH Reviewed; 611 AA.
AC Q84UU9; O04537;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Dolabella-3,7-dien-18-ol synthase TPS06 {ECO:0000305};
DE EC=4.2.3.167 {ECO:0000269|PubMed:27933080};
DE AltName: Full=Terpenoid synthase 6 {ECO:0000303|PubMed:12207221};
DE Short=AtTPS06 {ECO:0000303|PubMed:12207221};
GN Name=TPS06 {ECO:0000303|PubMed:12207221};
GN OrderedLocusNames=At1g70080 {ECO:0000312|Araport:AT1G70080};
GN ORFNames=F20P5.19 {ECO:0000312|EMBL:AAB61105.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
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 [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).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Cvi-0;
RX PubMed=27933080; DOI=10.3389/fpls.2016.01761;
RA Wang Q., Jia M., Huh J.H., Muchlinski A., Peters R.J., Tholl D.;
RT "Identification of a dolabellane type diterpene synthase and other root-
RT expressed diterpene synthases in Arabidopsis.";
RL Front. Plant Sci. 7:1761-1761(2016).
CC -!- FUNCTION: Involved in terpene biosynthesis in roots. Possesses
CC sesquiterpene (C15) synthase activity and diterpene (C20) synthase
CC activity in vitro. Possesses dolabella-3,7-dien-18-ol synthase activity
CC in vitro. Catalyzes the formation of dolabella-3,7-dien-18-ol from
CC geranylgeranyl diphosphate. {ECO:0000269|PubMed:27933080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (3E,7E)-
CC dolabella-3,7-dien-18-ol + diphosphate; Xref=Rhea:RHEA:16345,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:137565; EC=4.2.3.167;
CC Evidence={ECO:0000269|PubMed:27933080};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers but also in
CC stems, siliques, roots and leaves. {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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002062; AAB61105.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35014.1; -; Genomic_DNA.
DR EMBL; AF497486; AAO85534.1; -; mRNA.
DR PIR; E96723; E96723.
DR RefSeq; NP_177165.1; NM_105676.2.
DR AlphaFoldDB; Q84UU9; -.
DR SMR; Q84UU9; -.
DR STRING; 3702.AT1G70080.1; -.
DR PaxDb; Q84UU9; -.
DR PRIDE; Q84UU9; -.
DR ProteomicsDB; 245210; -.
DR EnsemblPlants; AT1G70080.1; AT1G70080.1; AT1G70080.
DR GeneID; 843344; -.
DR Gramene; AT1G70080.1; AT1G70080.1; AT1G70080.
DR KEGG; ath:AT1G70080; -.
DR Araport; AT1G70080; -.
DR TAIR; locus:2020658; AT1G70080.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q84UU9; -.
DR OMA; MQEAQWT; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q84UU9; -.
DR BioCyc; ARA:AT1G70080-MON; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q84UU9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84UU9; baseline and differential.
DR Genevisible; Q84UU9; AT.
DR GO; GO:0005737; C:cytoplasm; 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; IDA:TAIR.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IBA:GO_Central.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..611
FT /note="Dolabella-3,7-dien-18-ol synthase TPS06"
FT /id="PRO_0000403702"
FT MOTIF 363..367
FT /note="DDXXD motif; degenerate"
FT /evidence="ECO:0000305"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 11
FT /note="F -> S (in Ref. 3; AAO85534)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="K -> R (in Ref. 3; AAO85534)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> V (in Ref. 3; AAO85534)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="M -> I (in Ref. 3; AAO85534)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="I -> V (in Ref. 3; AAO85534)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="V -> G (in Ref. 3; AAO85534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 71112 MW; C68009865C923DEF CRC64;
MEAITKYGSY FNVRFLSRLC WRLNLSSSYH YPLLKSSLSF SRFQSPKKLC LVRATTNPTD
DNSTTRSFTP HPPSLWGHHF LSASVNQTEM DDLWRQIEAL KPIVNAMLLP CNGADAKKIT
CFIHTLVSLG VSYHFEEKIV EFLKDAFENI EDMIIDCKED DLYTVSIIFR VFRLYGHYIT
PDIFNRFKGD DGNFKKCLND DVRGMLSFYE ASHFGTTTED ILEEAMSFTQ KHLELFLVGE
KAKHYPHITK LIQAALYIPQ NFNLEILVAR EYIDFYELET DHNEMLLKLA KLNFRFLQLQ
YIQDLKTLTT WWKELDLVSK IPVYFRERLA EPYFWATGIY YEPQYSAARI MLAKSIILVD
IVDNTFDVYG TIDEVKSLVQ AIERWDSDAV DVLPDYLKVV FRTTFDLFKE LEEYVSSEAR
SFTMQYAYEQ LRILMKGYLQ EAEWSNRGHL PSHEEYIEVG VASTAGEVLL AMTFIPMGDA
AGVGVYEWLR SRPKLTHALF VKSRLRDDIA TYKEEMKRGD VCNGINCYTK QHKVSEEEAC
IEFEKKTNHM SKVMNEEFLK AAKFIPLHIL RPVLNYGRLA DVCYKYGDGY TFAGEKIKDY
ITSLYVDLIT L
