ID   DTCYA_STRSQ             Reviewed;         371 AA.
AC   M1V9Q0;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Diterpene cyclase DtcycA {ECO:0000303|PubMed:23386483};
DE   AltName: Full=Cembrene C synthase {ECO:0000305};
DE            EC=4.2.3.148 {ECO:0000269|PubMed:23386483};
DE   AltName: Full=Nephthenol synthase {ECO:0000305};
DE            EC=4.2.3.149 {ECO:0000269|PubMed:23386483};
GN   Name=dtcycA {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 = cembrene C +
CC         diphosphate; Xref=Rhea:RHEA:42988, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58756, ChEBI:CHEBI:82798; EC=4.2.3.148;
CC         Evidence={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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:23386483};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=93.7 uM for geranylgeranyl diphosphate
CC         {ECO:0000269|PubMed:23386483};
CC         Note=kcat is 2.8 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; AB738084; BAM78697.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1V9Q0; -.
DR   SMR; M1V9Q0; -.
DR   KEGG; ag:BAM78697; -.
DR   BRENDA; 4.2.3.148; 1284.
DR   BRENDA; 4.2.3.149; 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   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..371
FT                   /note="Diterpene cyclase DtcycA"
FT                   /id="PRO_0000435481"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ   SEQUENCE   371 AA;  41747 MW;  33420AE28AA90E23 CRC64;
     MTDPAVTPLA FSIPQLYCPF PTAIHPEVDT LTRAGMDFMT HHGFCNTEAD RLVVANIDAG
     AIVARWYPNP DFPVDRLQMV TDFLYLYFLI DDLRFEVINS DTGLAGPIAL FAQHLDLWEY
     PQAHRREELD LFHQAIHDLA SRMAELTTPT KAARMRRSIN GWFLALLREI ALFNDDHAVM
     AEEYLPIRVV TVASRLMIDV NGFICPAEVP GDEWYSLKVQ AAAEAAMSVC LYDNELYSAG
     KEQWLKSRAT AHDRRPRNLV ALIQAQTGGS TEHALQEVAE YRNRTVCLYL NLRSQLEKTA
     SPALLAYLSV LDGVISGNLD AHATSSRYHN PDGHHPHAIA FTPLRTTDEC SARAHTPIAP
     PIAWWWEQLD Q