TSUKU_STRT9
ID TSUKU_STRT9 Reviewed; 332 AA.
AC I2N045;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Tsukubadiene synthase {ECO:0000303|PubMed:28146322};
DE Short=TdS {ECO:0000303|PubMed:28146322};
DE EC=4.2.3.159 {ECO:0000269|PubMed:25605043, ECO:0000269|PubMed:28146322};
GN ORFNames=STSU_20912 {ECO:0000312|EMBL:EIF90392.1};
OS Streptomyces tsukubensis (strain DSM 42081 / NBRC 108919 / NRRL 18488 /
OS 9993).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1114943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993;
RX PubMed=22740677; DOI=10.1128/jb.00692-12;
RA Barreiro C., Prieto C., Sola-Landa A., Solera E., Martinez-Castro M.,
RA Perez-Redondo R., Garcia-Estrada C., Aparicio J.F.,
RA Fernandez-Martinez L.T., Santos-Aberturas J., Salehi-Najafabadi Z.,
RA Rodriguez-Garcia A., Tauch A., Martin J.F.;
RT "Draft genome of Streptomyces tsukubaensis NRRL 18488, the producer of the
RT clinically important immunosuppressant tacrolimus (FK506).";
RL J. Bacteriol. 194:3756-3757(2012).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993;
RX PubMed=25605043; DOI=10.1038/ja.2014.171;
RA Yamada Y., Arima S., Nagamitsu T., Johmoto K., Uekusa H., Eguchi T.,
RA Shin-ya K., Cane D.E., Ikeda H.;
RT "Novel terpenes generated by heterologous expression of bacterial terpene
RT synthase genes in an engineered Streptomyces host.";
RL J. Antibiot. 68:385-394(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND REACTION MECHANISM.
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993;
RX PubMed=28146322; DOI=10.1002/anie.201612439;
RA Rabe P., Rinkel J., Dolja E., Schmitz T., Nubbemeyer B., Luu T.H.,
RA Dickschat J.S.;
RT "Mechanistic investigations of two bacterial diterpene cyclases:
RT spiroviolene synthase and tsukubadiene synthase.";
RL Angew. Chem. Int. Ed. 56:2776-2779(2017).
CC -!- FUNCTION: Catalyzes the formation of the 5-9-5 ring skeleton
CC (3S,6S,11R,14S)-tsukubadiene from geranylgeranyl diphosphate (GGPP) via
CC a 1,11-cyclization and a 10Re,14Re-cyclization.
CC {ECO:0000269|PubMed:25605043, ECO:0000269|PubMed:28146322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate +
CC tsukubadiene; Xref=Rhea:RHEA:53624, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:137528; EC=4.2.3.159;
CC Evidence={ECO:0000269|PubMed:25605043, ECO:0000269|PubMed:28146322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Xaa-Glu (DDXXXE) and Ser-Xaa-Xaa-Xaa-Ser-
CC Xaa-Xaa-Xaa-Glu (SSE) motifs are important for the catalytic activity,
CC presumably through binding to Mg(2+). {ECO:0000305|PubMed:22740677}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CP029159; EIF90392.1; -; Genomic_DNA.
DR RefSeq; WP_006348711.1; NZ_AJSZ01000555.1.
DR AlphaFoldDB; I2N045; -.
DR SMR; I2N045; -.
DR EnsemblBacteria; EIF90392; EIF90392; STSU_20912.
DR PATRIC; fig|1114943.5.peg.4282; -.
DR OMA; EARAVEW; -.
DR BRENDA; 4.2.3.159; 14835.
DR Proteomes; UP000005940; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..332
FT /note="Tsukubadiene synthase"
FT /id="PRO_0000444977"
FT MOTIF 75..80
FT /note="DDXXXE motif"
FT /evidence="ECO:0000305|PubMed:22740677"
FT MOTIF 212..220
FT /note="SXXXSXXXE motif"
FT /evidence="ECO:0000305|PubMed:22740677"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 298..299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 332 AA; 37389 MW; A87D189A28E18373 CRC64;
MIEVPPFWCP LPIAIHPAAD QAEKDARAWA ERYGVRLRIA DQVQPGRLGA YWAPHGTYEG
MLAVGCWNFW AFAFDDHLDE PLPLDVPVTT SLVQQAVDIP SPPITDDPWA AGAQAVFNMF
RDLATPTQVR YCADNHRRWL HGACWRHSNH VNRRLPPLAE YIPLRMQDAA AQATCLIAVL
IGSDISVPEQ EMDSPRVRAL LETASWTATI DSDLHSFQLE DTQRPVSQHI VSVLMHERGI
GVDEALRQSV ALRDRFMTRF LHLQQECART GSSELARFAH TLGYVISGYL QWAVDTSRYG
QTEATFSFTD TPRDDTPEPP PGIPSVEWLW TL
