MTS17_SELML
ID MTS17_SELML Reviewed; 348 AA.
AC D8RLD3;
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=(+)-germacrene D synthase;
DE EC=4.2.3.77;
DE AltName: Full=Microbial Terpene synthase-like protein 17;
DE Short=SmMTPSL17;
DE EC=4.2.3.-;
GN ORFNames=SELMODRAFT_412756;
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 eight sesquiterpenes, with (+)-germacrene D and an unidentified
CC oxygenated sesquiterpene as the major products. Has no diterpene
CC synthase activity. {ECO:0000269|PubMed:22908266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate;
CC Xref=Rhea:RHEA:30427, ChEBI:CHEBI:33019, ChEBI:CHEBI:49046,
CC ChEBI:CHEBI:175763; EC=4.2.3.77;
CC Evidence={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: Not 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; JX413785; AFR34005.1; -; mRNA.
DR EMBL; GL377583; EFJ26899.1; -; Genomic_DNA.
DR RefSeq; XP_002971982.1; XM_002971936.1.
DR AlphaFoldDB; D8RLD3; -.
DR SMR; D8RLD3; -.
DR PRIDE; D8RLD3; -.
DR EnsemblPlants; EFJ26899; EFJ26899; SELMODRAFT_412756.
DR Gramene; EFJ26899; EFJ26899; SELMODRAFT_412756.
DR KEGG; smo:SELMODRAFT_412756; -.
DR eggNOG; ENOG502SJ0F; Eukaryota.
DR HOGENOM; CLU_042538_2_1_1; -.
DR InParanoid; D8RLD3; -.
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..348
FT /note="(+)-germacrene D synthase"
FT /id="PRO_0000421942"
FT MOTIF 97..101
FT /note="DDXXD motif"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 348 AA; 38990 MW; 9B82A3C5084931F6 CRC64;
MAVSSIASIF AAEKSYSIPP VCQLLVSPVL NPLYDAKAES QIDAWCAEFL KLQPGSEKAV
FVQESRLGLL AAYVYPTIPY EKIVPVGKFF ASFFLADDIL DSPEISSSDM RNVATAYKMV
LKGRFDEATL PVKNPELLRQ MKMLSEVLEE LSLHVVDESG RFVDAMTRVL DMFEIESSWL
RKQIIPNLDT YLWLREITSG VAPCFALIDG LLQLRLEERG VLDHPLIRKV EEIGTHHIAL
HNDLMSLRKE WATGNYLNAV PILASNRKCG LNEAIGKVAS MLKDLEKDFA RTKHEIISSG
LAMKQGVMDY VNGIEVWMAG NVEWGWTSAR YHGIGWIPPP EKSGTFQL
