TPS29_ARATH
ID TPS29_ARATH Reviewed; 607 AA.
AC Q9C6W6; F4IB08; Q9C6T3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Terpenoid synthase 29;
DE Short=AtTPS29;
DE EC=4.2.3.-;
GN Name=TPS29; OrderedLocusNames=At1g31950; ORFNames=F5M6.5, T12O21.14;
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 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).
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 flowers but also in
CC siliques, roots, leaves and stems. {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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50788.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC074309; AAG50788.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079041; AAG50729.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31421.2; -; Genomic_DNA.
DR PIR; G86443; G86443.
DR RefSeq; NP_001319127.1; NM_001332991.1.
DR RefSeq; NP_001320348.1; NM_001332993.1.
DR AlphaFoldDB; Q9C6W6; -.
DR SMR; Q9C6W6; -.
DR STRING; 3702.AT1G31950.1; -.
DR iPTMnet; Q9C6W6; -.
DR PaxDb; Q9C6W6; -.
DR PRIDE; Q9C6W6; -.
DR EnsemblPlants; AT1G31950.1; AT1G31950.1; AT1G31950.
DR GeneID; 840085; -.
DR Gramene; AT1G31950.1; AT1G31950.1; AT1G31950.
DR KEGG; ath:AT1G31950; -.
DR Araport; AT1G31950; -.
DR TAIR; locus:2034511; AT1G31950.
DR eggNOG; ENOG502SHPY; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q9C6W6; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q9C6W6; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9C6W6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6W6; baseline and differential.
DR Genevisible; Q9C6W6; 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; 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; 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..607
FT /note="Terpenoid synthase 29"
FT /id="PRO_0000403716"
FT MOTIF 358..362
FT /note="DDXXD motif"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 70324 MW; CD8300837447DC31 CRC64;
MEAIRIGFGL PNVHSVPLCL TTTRCLFPRQ RLLHSHTPSW KPAKQQDFFV ASSSKKSSDD
LESSLPTPHF SPSLWGDHFL SVSLNRAEFD ELEREIETTK PLARDKLMSS ESSDKEKIRL
IHLLVSMGIS YHFDKEIQDI LKHSFTKLDD IIVGEDDLET ISIMFEVFKL YGHKMSCDAF
DRFRGNDGRF KESLVRDFRG MLQLFEVAHL GTPCEVIMDE ALSFTRNHLE SLTSGNASTA
SPHLLKHIQN SLYIPRYCNI EVLVAREYIS YYEQEEGHDE ILLKFAKLNF NFCQFHYVQE
LKTLTKWWRD LDLASKLPYI RDRLVESHLV ALGPYFEPHY SLGRIIVAKI NMIMVVVDDT
YDAYATLPQV KALTECLQRW SIEVSDKLPD YLRIVLGSLF DVMGEIEREM RPLGRLYRVK
QVVEKIKIIT KAYQEIAKWA RTGHVSTFDE YMKVGVLTAG MADYAAYCFI GMEDINEKEA
FEWLNSNPLI IKHLTAMFRL ANDVGTYETE INRGEVANGL NCYMKQYGVT KEEASRELRK
MYVYRKKVVV EEFMNSHDHV PRQVLLRCLN IARIFDVFYT EGDGYSEPKG KIEHFMTSLY
LHPIPLS
