MTS22_SELML
ID MTS22_SELML Reviewed; 368 AA.
AC D8RNZ9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=(3S,6E)-nerolidol synthase;
DE EC=4.2.3.48;
DE AltName: Full=Microbial Terpene synthase-like protein 22;
DE Short=SmMTPSL22;
DE AltName: Full=S-linalool synthase;
DE EC=4.2.3.25;
GN ORFNames=SELMODRAFT_413294;
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY
RP ELICITOR, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22908266; DOI=10.1073/pnas.1204300109;
RA Li G., Kollner T.G., Yin Y., Jiang Y., Chen H., Xu Y., Gershenzon J.,
RA Pichersky E., Chen F.;
RT "Nonseed plant Selaginella moellendorfii has both seed plant and microbial
RT types of terpene synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14711-14715(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- FUNCTION: Sesquiterpene synthase converting farnesyl diphosphate to
CC nerolidol. Has also a monoterpene synthase activity, converting geranyl
CC diphosphate into linalool as the major product. Has no diterpene
CC synthase activity. {ECO:0000269|PubMed:22908266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (3S,6E)-nerolidol +
CC diphosphate; Xref=Rhea:RHEA:27530, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59958, ChEBI:CHEBI:175763;
CC EC=4.2.3.48; Evidence={ECO:0000269|PubMed:22908266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate;
CC Xref=Rhea:RHEA:24116, ChEBI:CHEBI:98, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.25;
CC Evidence={ECO:0000269|PubMed:22908266};
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 -!- INDUCTION: Up-regulated by alamethicin treatment.
CC {ECO:0000269|PubMed:22908266}.
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:0000250}.
CC -!- MISCELLANEOUS: Selaginella moellendorffii contains two distinct types
CC of functional terpene synthases (TPS) genes, the typical seed plants
CC TPS genes (SmTPSs) and a microbial type TPS genes (SmMTPSLs).
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JX413786; AFR34006.1; -; mRNA.
DR EMBL; GL377585; EFJ26173.1; -; Genomic_DNA.
DR RefSeq; XP_002972952.1; XM_002972906.1.
DR AlphaFoldDB; D8RNZ9; -.
DR SMR; D8RNZ9; -.
DR STRING; 88036.EFJ26173; -.
DR PRIDE; D8RNZ9; -.
DR EnsemblPlants; EFJ26173; EFJ26173; SELMODRAFT_413294.
DR GeneID; 9637292; -.
DR Gramene; EFJ26173; EFJ26173; SELMODRAFT_413294.
DR KEGG; smo:SELMODRAFT_413294; -.
DR eggNOG; ENOG502SM5W; Eukaryota.
DR HOGENOM; CLU_063343_0_0_1; -.
DR InParanoid; D8RNZ9; -.
DR OrthoDB; 1143139at2759; -.
DR BioCyc; MetaCyc:MON-17912; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034007; F:S-linalool synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..368
FT /note="(3S,6E)-nerolidol synthase"
FT /id="PRO_0000421943"
FT MOTIF 91..95
FT /note="DDXXE motif"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 41840 MW; AEB8C15254091567 CRC64;
MKDLFRISGV THFELPLLPN NIPFACHPEF QSISLKIDKW FLGKMRIADE TSKKKVLESR
IGLYACMMHP HAKREKLVLA GKHLWAVFLL DDLLESSSKH EMPQLNLTIS NLANGNSDED
YTNPLLALYR EVMEEIRAAM EPPLLDRYVQ CVGASLEAVK DQVHRRAEKS IPGVEEYKLA
RRATGFMEAV GGIMTEFCIG IRLSQAQIQS PIFRELLNSV SDHVILVNDL LSFRKEFYGG
DYHHNWISVL LHHSPRGTSF QDVVDRLCEM IQAEELSILA LRKKIADEEG SDSELTKFAR
EFPMVASGSL VWSYVTGRYH GYGNPLLTGE IFSGTWLLHP MATVVLPSKF RMDTMRFSLA
PKKRDSFP
