BCAS_SACES
ID BCAS_SACES Reviewed; 353 AA.
AC K0K750;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=(-)-beta-caryophyllene synthase ((2E,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:27829890};
DE EC=4.2.3.57 {ECO:0000269|PubMed:27829890};
DE AltName: Full=Beta-caryophyllene synthase {ECO:0000303|PubMed:27829890};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:27829890};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:27829890};
GN Name=ptlA; OrderedLocusNames=BN6_54650 {ECO:0000312|EMBL:CCH32724.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharothrix.
OX NCBI_TaxID=1179773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000312|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764;
RX PubMed=27829890; DOI=10.3762/bjoc.12.173;
RA Rabe P., Schmitz T., Dickschat J.S.;
RT "Mechanistic investigations on six bacterial terpene cyclases.";
RL Beilstein J. Org. Chem. 12:1839-1850(2016).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield the bicyclic sesquiterpene (2S,10R)-(-)-(E)-beta-
CC caryophyllene via a probable 1,10-cyclization, which could involve the
CC abstraction of the pyrophosphate from FPP to yield a (E,E)-
CC germacradienyl cation. {ECO:0000269|PubMed:27829890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:27829890};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:27829890}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp (DDXXD) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:27829890}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HE804045; CCH32724.1; -; Genomic_DNA.
DR RefSeq; WP_015102836.1; NC_019673.1.
DR AlphaFoldDB; K0K750; -.
DR SMR; K0K750; -.
DR STRING; 1179773.BN6_54650; -.
DR EnsemblBacteria; CCH32724; CCH32724; BN6_54650.
DR KEGG; sesp:BN6_54650; -.
DR PATRIC; fig|1179773.3.peg.5508; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR OMA; AMEHWVI; -.
DR OrthoDB; 1869158at2; -.
DR BioCyc; SESP1179773:BN6_RS26410-MON; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Reference proteome.
FT CHAIN 1..353
FT /note="(-)-beta-caryophyllene synthase ((2E,6E)-farnesyl
FT diphosphate cyclizing)"
FT /id="PRO_0000443246"
FT MOTIF 85..89
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27829890"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 320..321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 82
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 86
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 160
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 353 AA; 39205 MW; 1B165C3CD8BACA57 CRC64;
MGRPATPQQT AFHIPFPRAI SPDVSAVHPG SMAWLRRHGM LRSDASARRV DGWRLTELAG
RFFPDARGED LRLGADVMGF FFLFDDQFDH PGGLRAEAVA VSKRLLHLTS LPAGPAPEGA
GPVVAAWADL WNRSCQGMSS AWRVRAAREW RRYFVGNLEE SVAREGMSGE SVEDYLRLRA
MTIGTTPVYD LCERTQHFEI PDEVLHSHHV QAMRDLATEI VVLCNDVAST IKESARGETL
NAVLLLERHH EAERGPAVAR VQRMVEARLA AFRRLRDRTS RTCAALDLTA EQCDRVDRYV
RTALMSVVRG NYDWQQRSAR FSADDARPGS LPGYLDDLVG HSGVVGPPPV DGS
