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BCLTS_ALKCL
ID   BCLTS_ALKCL             Reviewed;         352 AA.
AC   M5AW86;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Trifunctional sesterterpene/triterpene/sesquarterpene synthase {ECO:0000303|PubMed:25882275};
DE            EC=4.2.3.188 {ECO:0000269|PubMed:23554321, ECO:0000269|PubMed:25882275};
DE   AltName: Full=Bcl-TS {ECO:0000303|PubMed:23554321};
DE   AltName: Full=Beta-geranylfarnesene synthase {ECO:0000305};
GN   Name=bcl-ts {ECO:0000303|PubMed:23554321};
OS   Alkalihalobacillus clausii (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=79880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=JCM 9138;
RX   PubMed=23554321; DOI=10.1002/cbic.201300035;
RA   Sato T., Yamaga H., Kashima S., Murata Y., Shinada T., Nakano C.,
RA   Hoshino T.;
RT   "Identification of novel sesterterpene/triterpene synthase from Bacillus
RT   clausii.";
RL   ChemBioChem 14:822-825(2013).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=JCM 9138;
RX   PubMed=25882275; DOI=10.1002/cbic.201500138;
RA   Ueda D., Yamaga H., Murakami M., Totsuka Y., Shinada T., Sato T.;
RT   "Biosynthesis of sesterterpenes, head-to-tail triterpenes, and
RT   sesquarterpenes in Bacillus clausii: identification of multifunctional
RT   enzymes and analysis of isoprenoid metabolites.";
RL   ChemBioChem 16:1371-1377(2015).
CC   -!- FUNCTION: Catalyzes the conversion of geranylfarnesyl diphosphate
CC       (GFPP) and hexaprenyl diphosphate (HexPP) into beta-geranylfarnesene
CC       and beta-hexaprene, respectively (PubMed:23554321, PubMed:25882275).
CC       Also produces beta-heptaprene from heptaprenyl diphosphate (HepPP) as a
CC       minor product (PubMed:25882275). {ECO:0000269|PubMed:23554321,
CC       ECO:0000269|PubMed:25882275}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E,14E)-geranylfarnesyl diphosphate = beta-
CC         geranylfarnesene + diphosphate; Xref=Rhea:RHEA:54500,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:138226;
CC         EC=4.2.3.188; Evidence={ECO:0000269|PubMed:23554321,
CC         ECO:0000269|PubMed:25882275};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-hexaprenyl diphosphate = beta-hexaprene +
CC         diphosphate; Xref=Rhea:RHEA:54504, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58179, ChEBI:CHEBI:138227; EC=4.2.3.188;
CC         Evidence={ECO:0000269|PubMed:23554321, ECO:0000269|PubMed:25882275};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-heptaprenyl diphosphate = beta-heptaprene +
CC         diphosphate; Xref=Rhea:RHEA:54508, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58206, ChEBI:CHEBI:138228; EC=4.2.3.188;
CC         Evidence={ECO:0000269|PubMed:25882275};
CC   -!- SIMILARITY: Belongs to the large terpene synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AB735674; BAN05296.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5AW86; -.
DR   SMR; M5AW86; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019712; YtpB-like.
DR   Pfam; PF10776; DUF2600; 1.
PE   1: Evidence at protein level;
KW   Lyase.
FT   CHAIN           1..352
FT                   /note="Trifunctional
FT                   sesterterpene/triterpene/sesquarterpene synthase"
FT                   /id="PRO_0000449800"
SQ   SEQUENCE   352 AA;  41386 MW;  32F06C256A706758 CRC64;
     MGTVPANPFK IIQLAFKETV PKAHAELQKW HQEALKIEDV EIREQAAWTV NDKTFHCEGG
     SIFALLAGEN KDNHIQFLVA YQTICDYLDT LCDKNDAHDP NDFRSIHQAL LDCLTPDKPY
     GDYYQYRDRF EDNGYLRKLV DACREATASF PGFADMQTHM QEVSQFYIDF QVYKHVEEEK
     REPLLKDFYE RNKHFAPTMR WYEFACGTAS TLALYCMAAY AAAPVQTAQG QQIKEAYFTW
     VQGVHILLDY FIDQEEDRQE NEMNFVAYYR DSKEMFERFK YIDEKATEKL QMLPDKKFHL
     LLKTGLYALY LSDKKVMSHP RLKAEAKQLI KLGGFPASLF YYNRWIFKRK IS
 
 
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