MTS1_SELML
ID MTS1_SELML Reviewed; 349 AA.
AC J9R1J8; D8QQD2;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Microbial Terpene synthase-like protein 1;
DE Short=SmMTPSL1;
DE EC=4.2.3.-;
GN ORFNames=SELMODRAFT_402353;
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 six
CC sesquiterpenes, with beta-elemene, delta-cadinene and an unidentified
CC oxygenated sesquiterpene as the major products. Has no diterpene
CC synthase activity. {ECO:0000269|PubMed:22908266}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(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; JX413784; AFR34004.1; -; mRNA.
DR EMBL; GL377565; EFJ38437.1; -; Genomic_DNA.
DR RefSeq; XP_002960898.1; XM_002960852.1.
DR AlphaFoldDB; J9R1J8; -.
DR SMR; J9R1J8; -.
DR PRIDE; J9R1J8; -.
DR EnsemblPlants; EFJ38437; EFJ38437; SELMODRAFT_402353.
DR GeneID; 9641730; -.
DR Gramene; EFJ38437; EFJ38437; SELMODRAFT_402353.
DR KEGG; smo:SELMODRAFT_402353; -.
DR eggNOG; ENOG502SJ0F; Eukaryota.
DR HOGENOM; CLU_042538_2_1_1; -.
DR InParanoid; J9R1J8; -.
DR OrthoDB; 1143139at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..349
FT /note="Microbial Terpene synthase-like protein 1"
FT /id="PRO_0000421940"
FT MOTIF 98..102
FT /note="DDXXD motif"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 321
FT /note="A -> T (in Ref. 1; AFR34004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39172 MW; D33E0C7EFD38634C CRC64;
MAILSIVSIF AAEKSYSIPP ASNKLLASPA LNPLYDAKAD AEINVWCDEF LKLQPGSEKS
VFIRESRLGL LAAYAYPSIS YEKIVPVAKF IAWLFLADDI LDNPEISSSD MRNVATAYKM
VFKGRFDEAA LLVKNQELLR QVKMLSEVLK ELSLHLVDKS GRFMNSMTKV LDMFEIESNW
LHKQIVPNLD TYMWLREITS GVAPCFAMLD GLLQLGLEER GVLDHPLIRK VEEIGTHHIA
LHNDLISFRK EWAKGNYLNA VPILASIHKC GLNEAIAMLA SMVEDLEKEF IGTKQEIISS
GLARKQGVMD YVNGVEVWMA ANAEWGWLSA RYHGIGWIPP PEKSGTFQL
