TPS7_SELML
ID TPS7_SELML Reviewed; 750 AA.
AC G1DGI7; D8SMM0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=(13E)-labda-7,13-dien-15-ol synthase;
DE Short=SmCPSKSL1;
DE EC=3.1.7.10;
DE AltName: Full=Labda-7,13E-dien-15-ol-producing bifunctional diterpene synthase;
DE AltName: Full=Terpene synthase 7;
DE Short=SmTPS7;
GN ORFNames=SELMODRAFT_120716;
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, AND CATALYTIC ACTIVITY.
RX PubMed=21751328; DOI=10.1002/cbic.201100336;
RA Mafu S., Hillwig M.L., Peters R.J.;
RT "A novel labda-7,13e-dien-15-ol-producing bifunctional diterpene synthase
RT from Selaginella moellendorffii.";
RL ChemBioChem 12:1984-1987(2011).
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).
RN [3]
RP 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).
CC -!- FUNCTION: Bifunctional diterpene synthase that directly generates the
CC endocyclic double bond, as well as the hydroxyl group: produces an
CC endocyclic double bond isomer of copalyl diphosphate (CPP), and carries
CC out subsequent replacement of the diphosphate by a hydroxyl group to
CC form (13E)-labda-7,13-dien-15-ol. {ECO:0000269|PubMed:21751328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + H2O = (13E)-labda-7,13-dien-15-ol
CC + diphosphate; Xref=Rhea:RHEA:32075, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:63683; EC=3.1.7.10;
CC Evidence={ECO:0000269|PubMed:21751328};
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 -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) and Asp-Asp-Xaa-Xaa-Asp/Glu
CC (DDXXD/E) motifs are important for the catalytic activities, presumably
CC through binding to Mg(2+). {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=EFJ14208.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JN001323; AEK75338.1; -; mRNA.
DR EMBL; GL377628; EFJ14208.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002984563.1; XM_002984517.1.
DR AlphaFoldDB; G1DGI7; -.
DR SMR; G1DGI7; -.
DR STRING; 88036.EFJ14208; -.
DR PRIDE; G1DGI7; -.
DR KEGG; smo:SELMODRAFT_120716; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; G1DGI7; -.
DR OrthoDB; 372122at2759; -.
DR BRENDA; 3.1.7.10; 9844.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0102305; F:(13E)-labda-7,13-dien-15-ol 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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..750
FT /note="(13E)-labda-7,13-dien-15-ol synthase"
FT /id="PRO_0000418754"
FT MOTIF 284..287
FT /note="DXDD motif"
FT MOTIF 501..505
FT /note="DDXXD motif"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 651
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 655
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 748
FT /note="P -> A (in Ref. 1; AEK75338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 750 AA; 86619 MW; D144F64499966475 CRC64;
MIEEMRKLLA TLDDGEISPS AYDTAWVARI PSQSNATCPE FPETLEWIAH NQLPDGSWGD
RNHFQIYDRV LSTVSCLVAL KTWNLGHDNI NKGERFLKQN IYKLTKDKGD LLCGFELIFM
TMLEEAKQKG LDIPIDIPAL KILQGYRQKK LQKIPLEMVH SIPTTILYSL EGLQDHINWE
KILQFIGTDG SFLSSPSATA CVYMHTKDPR CLEYLKGVVK KVKNSVPCQY AIDLFERLWI
VDTLERLGID RYFQPEIKNI LDYVYKYWSD KKGIGWGRES YLKDIDDTSM GFRLLRLHGY
KVTPDVFLNF MSSEDKFFCF PGESYHGASD IFNLYRASQV AFANDNILTK AKNYAHKYLS
QLDKAYLDKW SAKKNFFQEV EFELSNQWNS CLPRAYSKSY IHNYGPNDIW IAKTIYRLPF
VNNELFINLA KEDFNACQSI HQSEIQTLLR WWAALKFGDL PFFGDKVVTA HFSIASCMFE
PEFSELRLFY TKYALLSSTL DDLADYYGSP AQTRCILEAI RSWDPSLVSH LSEEVQICFS
GLYRTINEMV KSASKVQTGS SINIREHMQE QLAKLISAQL VDAEWMERKH IPSFETYLSN
ATVSVGMQDL LLSSIFFCGE SISKHLMQEI KNSRCLQLTC LIARLCNDIG TYQFEREKGE
VASSITCYMR ENRGITESQA IEHLQGIIDE SWKELTEEFL TPSQIPRSIK RLMFETARIF
QFIYPKKDNF KDPSKAMASL IQNVLYKPAE
