MTS26_SELML
ID MTS26_SELML Reviewed; 367 AA.
AC J9QS25; D8RT78;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=(E)-2-epi-beta-caryophyllene synthase;
DE EC=4.2.3.137;
DE AltName: Full=Microbial Terpene synthase-like protein 26;
DE Short=SmMTPSL26;
GN ORFNames=SELMODRAFT_414574;
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 (E)-2-epi-beta-caryophyllene as the major product, and to two other
CC unidentified sesquiterpenes. Has no diterpene synthase activity.
CC {ECO:0000269|PubMed:22908266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-2-epi-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:34703, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:68667, ChEBI:CHEBI:175763; EC=4.2.3.137;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFJ24463.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JX413787; AFR34007.1; -; mRNA.
DR EMBL; GL377589; EFJ24463.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002974241.1; XM_002974195.1.
DR AlphaFoldDB; J9QS25; -.
DR SMR; J9QS25; -.
DR STRING; 88036.EFJ24631; -.
DR PRIDE; J9QS25; -.
DR KEGG; smo:SELMODRAFT_414574; -.
DR eggNOG; ENOG502T11A; Eukaryota.
DR InParanoid; J9QS25; -.
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..367
FT /note="(E)-2-epi-beta-caryophyllene synthase"
FT /id="PRO_0000421944"
FT MOTIF 93..97
FT /note="DDXXE motif"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 366
FT /note="T -> M (in Ref. 1; AFR34007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 42064 MW; 009B37FF60FBF312 CRC64;
MEDVLAEKLS RVCKFDLPFI PCSIPFECHP DFTRISKDTD AWALRMLSIT DPYERKKALQ
GRHSLYSPMI IPRGESSKAE LSSKHTWTMF VLDDIAENFS EQEGKKAIDI LLEVAEGSYV
LSEKEKEKHP SHAMFEEVMS SFRSLMDPPL FARYMNCLRN YLDSVVEEAS LRIAKSIPSL
EKYRLLRRET SFMEADGGIM CEFCMDLKLH KSVVESPDFV AFVKAVIDHV VLVNDLLSFR
HELKIKCFHN YLCVIFCHSP DNTSFQETVD KVCEMIQEAE AEILQLQQKL IKLGEETGDK
DLVEYATWYP CVASGNLRWS YVTGRYHGLD NPLLNGEPFQ GTWFLHPEAT LILPLGSKCG
NHPFITI
