ID   DTCYB_STRSQ             Reviewed;         343 AA.
AC   M1VDX3;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Diterpene cyclase DtcycB {ECO:0000303|PubMed:23386483};
DE   AltName: Full=Cembrene A synthase {ECO:0000305};
DE            EC=4.2.3.150 {ECO:0000269|PubMed:23386483};
DE   AltName: Full=Nephthenol synthase {ECO:0000305};
DE            EC=4.2.3.149 {ECO:0000269|PubMed:23386483};
DE   AltName: Full=Pentamethylcyclopentadecatrienol synthase {ECO:0000305};
DE            EC=4.2.3.151 {ECO:0000269|PubMed:23386483};
GN   Name=dtcycB {ECO:0000303|PubMed:23386483};
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=SANK 60404;
RX   PubMed=23386483; DOI=10.1002/cbic.201200651;
RA   Meguro A., Tomita T., Nishiyama M., Kuzuyama T.;
RT   "Identification and characterization of bacterial diterpene cyclases that
RT   synthesize the cembrane skeleton.";
RL   ChemBioChem 14:316-321(2013).
CC   -!- FUNCTION: Diterpene cyclases that can form multiple diterpene products.
CC       {ECO:0000269|PubMed:23386483}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (R)-nephthenol
CC         + diphosphate; Xref=Rhea:RHEA:42992, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:82799;
CC         EC=4.2.3.149; Evidence={ECO:0000269|PubMed:23386483};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (R)-cembrene A +
CC         diphosphate; Xref=Rhea:RHEA:42996, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58756, ChEBI:CHEBI:82800; EC=4.2.3.150;
CC         Evidence={ECO:0000269|PubMed:23386483};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (1S,4E,8E,12E)-
CC         2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol + diphosphate;
CC         Xref=Rhea:RHEA:43000, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58756, ChEBI:CHEBI:82801; EC=4.2.3.151;
CC         Evidence={ECO:0000269|PubMed:23386483};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:23386483};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=42.1 uM for geranylgeranyl diphosphate
CC         {ECO:0000269|PubMed:23386483};
CC         Note=kcat is 1.3 min(-1). {ECO:0000269|PubMed:23386483};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23386483}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AB738085; BAM78698.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1VDX3; -.
DR   SMR; M1VDX3; -.
DR   PRIDE; M1VDX3; -.
DR   KEGG; ag:BAM78698; -.
DR   BRENDA; 4.2.3.149; 1284.
DR   BRENDA; 4.2.3.150; 1284.
DR   BRENDA; 4.2.3.151; 1284.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..343
FT                   /note="Diterpene cyclase DtcycB"
FT                   /id="PRO_0000435482"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ   SEQUENCE   343 AA;  37887 MW;  BF547FFC59F0BCB7 CRC64;
     MDLPPALLSF YCPIASEVSP EHEAVAQEMY AWIHAMSLTS DNRQAKMLAQ AGAGFNSYFT
     PRARGELARA LSKYNVCAWI ANGMVQEIRD PGTFGAMAAR WARIMEEPAT CPADGIPMDF
     ALADAFSHIR RTLSPVKWQH FSAAQSHWMH GLAWENCLHQ VKGLTVHDYL SFRYVMSGCF
     AAAAFAYAVP ERHPSAEEWA HPKVRAAADA AMMVDALDND RYSYLKESLT EADKKTIFAA
     LRHENPALGR EEVIVRGVQL RDRILTLYLT LRGELLCDAS EGLRSYLTGL DLIIAGNLVF
     CADMGLRYGL PEGSVRTDAE PLDRTVAPPG IGAIDHWWAQ AGA