ID   RMND_STRAQ              Reviewed;         322 AA.
AC   A0A0H5BN61;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=(12E)-labda-8(17),12,14-triene synthase {ECO:0000303|PubMed:26507838};
DE            EC=4.2.3.193 {ECO:0000269|PubMed:26507838};
DE   AltName: Full=Type-A diterpene synthase {ECO:0000303|PubMed:26507838};
GN   Name=rmnD {ECO:0000303|PubMed:26507838};
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RC   STRAIN=GM95 {ECO:0000312|EMBL:BAR97463.1};
RX   PubMed=26507838; DOI=10.1007/s10295-015-1694-6;
RA   Ikeda H., Shin-ya K., Nagamitsu T., Tomoda H.;
RT   "Biosynthesis of mercapturic acid derivative of the labdane-type diterpene,
RT   cyslabdan that potentiates imipenem activity against methicillin-resistant
RT   Staphylococcus aureus: cyslabdan is generated by mycothiol-mediated
RT   xenobiotic detoxification.";
RL   J. Ind. Microbiol. Biotechnol. 43:325-342(2016).
CC   -!- FUNCTION: Involved in the biosynthesis of the labdane-type bicyclic
CC       diterpene labda-8(17),12(E),14-triene. Catalyzes the conversion of (+)-
CC       copalyl diphosphate to yield labda-8(17),12(E),14-triene.
CC       {ECO:0000269|PubMed:26507838}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-copalyl diphosphate = (12E)-labda-8(17),12,14-triene +
CC         diphosphate; Xref=Rhea:RHEA:54640, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58635, ChEBI:CHEBI:138302; EC=4.2.3.193;
CC         Evidence={ECO:0000250|UniProtKB:A0A0H5BN57};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A0H5BN57};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Xaa-Glu (DDXXXE) 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:26507838}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC   -!- CAUTION: Not expressed under laboratory conditions.
CC       {ECO:0000269|PubMed:26507838}.
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; LC064029; BAR97463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5BN61; -.
DR   SMR; A0A0H5BN61; -.
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   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..322
FT                   /note="(12E)-labda-8(17),12,14-triene synthase"
FT                   /id="PRO_0000444808"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           93..98
FT                   /note="DDXXXE motif"
FT                   /evidence="ECO:0000305|PubMed:26507838"
FT   MOTIF           234..242
FT                   /note="NXXXSXXXE motif"
FT                   /evidence="ECO:0000305|PubMed:26507838"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         188
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         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT   BINDING         319..320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   322 AA;  35384 MW;  EB1245595C777980 CRC64;
     MNDATRTSTT PPALPMPDLR DSFPGPFPAS AHADDIERHA TQWLRTFPLI RSERALSALT
     HITGQGVART FPTAGRDELF LCADLFLWLT AFDDAHGEAT GAADPARLLR TTSEYVHLLA
     GHHEPPGGPS VFGAALRDLL DRYGERATPA QYARLTAHLR DNLFGILWEA HHLHRPDRVT
     LPDYLAMRPH TVFVRTVVAT AEVMLGYELT EPDRSSEPVR ELETAVADLA GWINDLASYA
     KETARDGSAT LGLPALLMRQ HECDLEEAFR RASLMCEQQA AVAAARIAEL TAGGGPLADH
     AHALRSVASS YVWHIDDSRY RT