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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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