TPS9_SELML
ID TPS9_SELML Reviewed; 739 AA.
AC J9QS23; D8QQZ1;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Copalyl diphosphate synthase 1;
DE EC=5.5.1.12;
DE AltName: Full=Terpene synthase 9;
DE Short=SmTPS9;
GN Name=CPS1; ORFNames=SELMODRAFT_402532;
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, GENE FAMILY, AND
RP 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: Monofunctional diterpene synthase converting geranylgeranyl
CC diphosphate to copalyl diphosphate. {ECO:0000269|PubMed:22908266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:58756; EC=5.5.1.12;
CC Evidence={ECO:0000269|PubMed:22908266};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity, presumably through binding to Mg(2+). {ECO:0000250}.
CC -!- MISCELLANEOUS: S.moellendorffii contains two distinct types of
CC functional terpene synthases (TPS) genes, the typical seed plants TPS
CC genes (SmTPSs) and the microbial type TPS genes (SmMTPSLs).
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFJ37889.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JX413782; AFR34002.1; -; mRNA.
DR EMBL; GL377565; EFJ37889.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002960350.1; XM_002960304.1.
DR AlphaFoldDB; J9QS23; -.
DR SMR; J9QS23; -.
DR STRING; 88036.EFJ37888; -.
DR PRIDE; J9QS23; -.
DR EnsemblPlants; EFJ37889; EFJ37889; SELMODRAFT_402532.
DR GeneID; 9655852; -.
DR Gramene; EFJ37889; EFJ37889; SELMODRAFT_402532.
DR KEGG; smo:SELMODRAFT_402532; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; J9QS23; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR GO; GO:0016102; P:diterpenoid 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; 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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Isomerase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..739
FT /note="Copalyl diphosphate synthase 1"
FT /id="PRO_0000421938"
FT MOTIF 287..290
FT /note="DXDD motif"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
SQ SEQUENCE 739 AA; 84560 MW; 081E0E34C777DDBE CRC64;
MWELVETVRS MLNSLHDGEI SVSAYDTAWV ARVPALDGSN TPQFPMCLNW IMNNQLEDGS
WGDRDLFLTY DRICSALACA IALKTWNTGD KIVHKALEFI RKTMPKMELE DSTHMPIGFE
IVFPAMIEEA MALELDIDYT APVLQTIYAE RKKKLERIPM NVVQNYPTTL LHSLEGLHKT
IDWDKVIKLQ SPDGSLLFSP ASTACALMHT GNEKCLQYLN NLVKRFNCAV PNVYPVDLFE
HLWIVDRLQR LGISRYFTQE IKSALDYVYR YWTDKGIAWA RGSPVQDADD TSMAFRLLRS
HGYDISPDAF KTFQEGDSFV CFSGQAGQAV TGMYNLYRAS QVMFPGETIL EEAGSFARKF
LEGKRQENQL YDKWIISKDL PGEVEFALDN PMHARLERLA TRRYIDQYAA DDVWIGKSLY
RMPFVNNPIF LELAKADFNM CRALHRKEFQ QLERWYDESS LSMFKGFSRS KLEQTFYSAA
ATIFEPELSP ARLIWSQCWF LSLGINEYFD YQGSTKELED LINNVERWNV NSLGNCSAKV
KILFVELYNI VQNHSKQGFL YQGRSIGGAL REIWKTWLSS LLQRTKWKMS DNYPTLEEYL
KASHSSIEPA VRSTVYFVGE TLATGDLKDS AICQMMNTAS RLVQDTHTDK VDSSLNSITI
YLEENPQLTE SEALSQVQAL ANKNMQKLLY ETLQPGALPQ ACKQLFLNAA RIMNVFPGTN
KVQAKLSNHV KRVLSQPVL
