ID   SPVIS_STRVB             Reviewed;         359 AA.
AC   P0DPK6;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Spiroviolene synthase {ECO:0000303|PubMed:28146322};
DE            Short=SvS {ECO:0000303|PubMed:28146322};
DE            EC=4.2.3.158 {ECO:0000269|PubMed:28146322};
OS   Streptomyces violens (Chainia violens).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=66377;
RN   [1]
RP   FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND REACTION MECHANISM.
RC   STRAIN=ATCC 15898 / DSM 40597 / NRRL ISP-5597;
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 (3R,6R,10S,11R,14R)-spiroviolene
CC       from geranylgeranyl diphosphate (GGPP) via a 1,11-cyclization and a
CC       10Re,14Si-cyclization. {ECO:0000269|PubMed:28146322}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (-)-spiroviolene +
CC         diphosphate; Xref=Rhea:RHEA:53620, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58756, ChEBI:CHEBI:137523; EC=4.2.3.158;
CC         Evidence={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-Asp (DDXXXD) and Asn-Xaa-Xaa-Xaa-Ser-
CC       Xaa-Xaa-Xaa-Glu (NSE) motifs are important for the catalytic activity,
CC       presumably through binding to Mg(2+). {ECO:0000305|PubMed:28146322}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   RefSeq; WP_030261827.1; NZ_JOBH01000013.1.
DR   AlphaFoldDB; P0DPK6; -.
DR   SMR; P0DPK6; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..359
FT                   /note="Spiroviolene synthase"
FT                   /id="PRO_0000444978"
FT   MOTIF           85..90
FT                   /note="DDXXXD motif"
FT                   /evidence="ECO:0000305|PubMed:28146322"
FT   MOTIF           226..234
FT                   /note="NXXXSXXXE motif"
FT                   /evidence="ECO:0000305|PubMed:28146322"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         312..313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   359 AA;  39968 MW;  0ECDB51A64EBC0F8 CRC64;
     MTVNEIDLPP IFCPLESARH PRAHLVDERA REWIRTSPMC TTDEERTWVA ASCSTDFFAR
     FAPDAATDDR LLWTSLWVYW GFAFDDHRCD NGPFSNRPAA FSALAGRVQR ALEAPSARDE
     SDGFIPALQE IAAQFRSFGT PLQVRRFAAA HRAWLSGVTW QIGNAAAGRM PGLDEYVAMR
     LLSAGGEPPF AMLELATGLE VPAQDLERPA VRALTEMAIM VAALDNDRHS LRKELARGQT
     DQNVYSVLMQ ETGLPLQEAV AAATRLRDRV LLRFMAVHDR VRPGAGLELS TYLQGLRYGI
     RGNAEWGLRV PRYLSLGRVP DPMDEAPLEW AESPADDDRS APRGLPTVAW WWDDALLGV