TPS4_SELML
ID TPS4_SELML Reviewed; 867 AA.
AC G9MAN7; D8R8K9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Bifunctional diterpene synthase, chloroplastic;
DE AltName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12;
DE AltName: Full=Miltiradiene synthase;
DE Short=SmMDS;
DE EC=4.2.3.131;
DE AltName: Full=Terpene synthase 4;
DE Short=SmTPS4;
DE Flags: Precursor;
GN Name=MDS; ORFNames=SELMODRAFT_450918;
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, AND MUTAGENESIS
RP OF 391-ASP-ASP-392 AND 611-ASP-ASP-612.
RX PubMed=22027823; DOI=10.1074/jbc.m111.302703;
RA Sugai Y., Ueno Y., Hayashi K., Oogami S., Toyomasu T., Matsumoto S.,
RA Natsume M., Nozaki H., Kawaide H.;
RT "Enzymatic (13)C labeling and multidimensional NMR analysis of miltiradiene
RT synthesized by bifunctional diterpene cyclase in Selaginella
RT moellendorffii.";
RL J. Biol. Chem. 286:42840-42847(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 cyclase that catalyzes the successive
CC two-step type-B (protonation-initiated cyclization) and type-A
CC (ionization-initiated cyclization) reactions of geranylgeranyl
CC diphosphate (GGDP) producing successively (+)-copalyl diphosphate and
CC miltiradiene. {ECO:0000269|PubMed:22027823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene;
CC Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:65037; EC=4.2.3.131;
CC Evidence={ECO:0000269|PubMed:22027823};
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:22027823};
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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: 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=EFJ31716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB668998; BAL41682.1; -; mRNA.
DR EMBL; GL377573; EFJ31716.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002967117.1; XM_002967071.1.
DR AlphaFoldDB; G9MAN7; -.
DR SMR; G9MAN7; -.
DR STRING; 88036.EFJ31716; -.
DR PRIDE; G9MAN7; -.
DR KEGG; smo:SELMODRAFT_450918; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR InParanoid; G9MAN7; -.
DR OrthoDB; 372122at2759; -.
DR BioCyc; MetaCyc:GIO6-20123-MON; -.
DR BRENDA; 5.5.1.12; 9844.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050559; F:copalyl diphosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0062205; F:miltiradiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR GO; GO:1901949; P:5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901948; P:5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:1901946; P:miltiradiene biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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 Chloroplast; Isomerase; Lyase; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..867
FT /note="Bifunctional diterpene synthase, chloroplastic"
FT /id="PRO_0000421937"
FT MOTIF 389..392
FT /note="DXDD motif"
FT MOTIF 611..615
FT /note="DDXXD motif"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MUTAGEN 391..392
FT /note="DD->GG: Can use only (+)-copalyl diphosphate as
FT substrate."
FT /evidence="ECO:0000269|PubMed:22027823"
FT MUTAGEN 611..612
FT /note="DD->GG: Produces only (+)-copalyl diphosphate."
FT /evidence="ECO:0000269|PubMed:22027823"
FT CONFLICT 28
FT /note="I -> T (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="R -> S (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="G -> E (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> P (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="L -> I (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="D -> G (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="P -> T (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="R -> K (in Ref. 1; BAL41682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 867 AA; 99915 MW; E567678D003D28D0 CRC64;
MAKVLFSSFQ QTGISGSLKS GQLSGVFING TNLKSNAHAK RFRKNSTSSI TIRCCASNSP
TLENTKLAGA PEKRQKKKQL PYQGILHVPG DRVEELDTRE TSLLVAEVKG WLMKLASGKG
EISPSAYDTA WVARIASESD SSLPEFPEAL EWIINSQLPD GSWGDDRHLQ LYDRVLSTLS
CLVTLKTWDI GHNSIAQGTK FLRENMIKLK QDDGDLLSGF EVTFPMMLHE AKQLGLDIPY
ETEFTRLLEI STKKKLAKIP LDKLHSAPTT LLYSLEGLQD LEIDWQKILK LQSKDGSFLS
SPSSTACVYL KTKDRKSLQY LQNAMEDQNY AVPCHYPIDL FESLWVVDTI ERLGIDVFFR
DEIKAVLDYV YSFWTNEGIG WGSTCLVNDI DDTAMAFRIL RMHGYNVSPD AFNQFWLPGD
KFCCFVGELS HGVSEMLNLH RASQVDFPNE AILTKTFKYS HDYLLNVDSA HMDKWATKKN
LMGEVAFELA NPFHDCLPRI YNNAYIKHYG MDDLWIAKTI YRLPLVNNKV FLELANRYAQ
QCQLYQPAEL TKLVNWWHSS RFEDIPSTRL TANIDMLPYI YYVICATFHE QEFAQLRVFF
SKACCLNTLF DDLMDCATSI EELDRLQNVI ERWDISLSHE LPLEYRIPFQ EFYNTVLVMT
EAASKIHKNL SPEFICKYLS GIYTKLIKSE IADARWKIEG YIPSFEEYME NAEVSISTWV
HVLMSILFCG EPLTEEILNT IYDSRPLKLD RIICRLCNDI QTYKIEMKLG QPTQGVSCYM
KEHPGATEED ALVYLQSLLE KTKRELNESY FITHENDLPK NIKRFNFEMV RMMLITYNET
RQVDLFRNPD NELKDMIKFC LETYRTL
