ID   LADIS_STRCL             Reviewed;         545 AA.
AC   D5SJ87;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Labda-7,13-dienyl diphosphate synthase {ECO:0000303|PubMed:26814669};
DE            EC=5.5.1.30 {ECO:0000305|PubMed:26814669};
DE   AltName: Full=Type-B diterpene synthase {ECO:0000303|PubMed:26814669};
GN   ORFNames=SCLAV_p0490 {ECO:0000312|EMBL:EFG03980.2};
OS   Streptomyces clavuligerus.
OG   Plasmid pSCL4 {ECO:0000312|EMBL:EFG03980.2,
OG   ECO:0000312|Proteomes:UP000002357}.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602 {ECO:0000312|Proteomes:UP000002357};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA   Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DOMAIN.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=26814669; DOI=10.1038/ja.2015.147;
RA   Yamada Y., Komatsu M., Ikeda H.;
RT   "Chemical diversity of labdane-type bicyclic diterpene biosynthesis in
RT   Actinomycetales microorganisms.";
RL   J. Antibiot. 69:515-523(2016).
CC   -!- FUNCTION: Involved in the biosynthesis of the labdane-type bicyclic
CC       diterpene labda-7,13(16),14-triene. Catalyzes the conversion of
CC       geranylgeranyl diphosphate (GGDP) into labda-7,13(E)-dienyl
CC       diphosphate. {ECO:0000269|PubMed:26814669}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (13E)-labda-7,13-
CC         dien-15-yl diphosphate; Xref=Rhea:RHEA:54692, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:63682; EC=5.5.1.30;
CC         Evidence={ECO:0000305|PubMed:26814669};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:26814669};
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp-Thr-Ala (DXDDTA) and Arg-Xaa-Xaa-Asp-Gly-
CC       Ser-Trp (RXXDGSW) motifs are expected to bind to Mg(2+).
CC       {ECO:0000305|PubMed:26814669}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; CM000914; EFG03980.2; -; Genomic_DNA.
DR   RefSeq; WP_003963126.1; NZ_CP027859.1.
DR   AlphaFoldDB; D5SJ87; -.
DR   SMR; D5SJ87; -.
DR   STRING; 443255.SCLAV_p0490; -.
DR   KEGG; ag:EFG03980; -.
DR   eggNOG; COG1657; Bacteria.
DR   OMA; RWHASPY; -.
DR   OrthoDB; 260889at2; -.
DR   BRENDA; 5.5.1.30; 5988.
DR   Proteomes; UP000002357; Plasmid pSCL4.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR032696; SQ_cyclase_C.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Magnesium; Metal-binding; Plasmid; Reference proteome.
FT   CHAIN           1..545
FT                   /note="Labda-7,13-dienyl diphosphate synthase"
FT                   /id="PRO_0000444809"
FT   REGION          526..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           315..320
FT                   /note="DXDDTA motif"
FT                   /evidence="ECO:0000305|PubMed:26814669"
FT   MOTIF           444..450
FT                   /note="RXXDGSW motif"
FT                   /evidence="ECO:0000305|PubMed:26814669"
SQ   SEQUENCE   545 AA;  58120 MW;  F6D66C8F44809D46 CRC64;
     MPVDVGTLPP PAPREAVSAA AHLLASVDGD PWGRTSPTVY ETARVHAWAP HLPGRDRRVT
     WLLDQQRAGG LWGDGPPAYQ VLPTLAAVTA LLAELDRHPE AGHSSLGGRL AAAVAAGLDT
     LHGLSHHDPL PDTAAVELLV PGLITEVNDR LDAIDPEAAH PALAPVPHGR RLTAVHGIPA
     LPRHRLAERL ARFARLPVKL HHCFEALAPV CPPGLVPARP DHLLGSSSAA TAAWLATATA
     APGAPGLDRL LRSTAARYGG LFPETARITV FERLWVLTTL HRAGLLATFE PLARRWVSAL
     AAPGGVPGVP GFEPDADDTA VTLHLATELG VPYRPEVLDP FRTGDHFACY LGEDTGSVST
     NAHVLLALGT WTRHHPDTAD HGNTIRLLGR WLVERQHGDG HWDDKWHASP YYATAKVTAA
     LSRHGGPEAA DALRRAARWV RETRRTDGSW GIWGGTAEET AYAAQILLDA PEPPTDVLGC
     AHAHLTARAD DDGPPPALWH DKTLFAPDAI VRAEVLSTLR RLDRRLPAPA PVPPGFDAAR
     TGPAD