LATES_STRCL
ID LATES_STRCL Reviewed; 343 AA.
AC B5GRC8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Labda-7,13(16),14-triene synthase {ECO:0000303|PubMed:26814669};
DE EC=4.2.3.192 {ECO:0000305|PubMed:26814669};
DE AltName: Full=Type-A diterpene synthase {ECO:0000303|PubMed:26814669};
GN ORFNames=SCLAV_p0491 {ECO:0000312|EMBL:EFG03981.2},
GN SSCG_01902 {ECO:0000312|EMBL:EDY48874.1};
OS Streptomyces clavuligerus.
OG Plasmid pSCL4 {ECO:0000312|EMBL:EFG03981.2,
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:UP000006569};
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces clavuligerus ATCC 27064.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
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};
RC PLASMID=pSCL4 {ECO:0000312|EMBL:EFG03981.2};
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 [3]
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 labda-
CC 7,13(E)-dienyl diphosphate to yield labda-7,13(16),14-triene.
CC {ECO:0000269|PubMed:26814669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13E)-labda-7,13-dien-15-yl diphosphate = diphosphate + labda-
CC 7,13(16),14-triene; Xref=Rhea:RHEA:54636, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:63682, ChEBI:CHEBI:138301; EC=4.2.3.192;
CC Evidence={ECO:0000305|PubMed:26814669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:26814669};
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:26814669}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; DS570635; EDY48874.1; -; Genomic_DNA.
DR EMBL; CM000914; EFG03981.2; -; Genomic_DNA.
DR RefSeq; WP_003954347.1; NZ_CP027859.1.
DR AlphaFoldDB; B5GRC8; -.
DR SMR; B5GRC8; -.
DR STRING; 443255.SCLAV_p0491; -.
DR EnsemblBacteria; EDY48874; EDY48874; SSCG_01902.
DR KEGG; ag:EFG03981; -.
DR OMA; LWERTND; -.
DR OrthoDB; 1082373at2; -.
DR BRENDA; 4.2.3.192; 5988.
DR Proteomes; UP000002357; Plasmid pSCL4.
DR Proteomes; UP000006569; Unassembled WGS sequence.
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 SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Plasmid; Reference proteome.
FT CHAIN 1..343
FT /note="Labda-7,13(16),14-triene synthase"
FT /id="PRO_0000444806"
FT MOTIF 114..119
FT /note="DDXXXE motif"
FT /evidence="ECO:0000305|PubMed:26814669"
FT MOTIF 252..260
FT /note="NXXXSXXXE motif"
FT /evidence="ECO:0000305|PubMed:26814669"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 343 AA; 37335 MW; 31B0AC4DD9BC3A1A CRC64;
MGRRARSARS FGVSPLWGGV SVRSGDRGEA AVGGLWEVPD FWGLFPSRIS PLAGEVESGT
RVWLDGWRLV EEAGPGERLK ASKVGRLVAL AYPDAPADLL RWAADLFAWL TAFDDVHVEA
PGVTTAELGP HMASFVGVLE TGTAPGAAPT PFPAALAELL DRARELLTPL QEERVRARLG
KVFVAMLWEI TTRERTVSTA EYETMRPHTF FSAVGAALVE PCAGLDLSHG VRADPGVRRL
TQALATLWER TNDLYSFAYE QRALGSVPRT LPWLIAQERG LPLDAAFAEA GRWCEEEAVL
AHRLIGELSA SAREGVPEYA GAVAHAIGGT RRLYEVSDRW REE
