GCOA_STRGG
ID GCOA_STRGG Reviewed; 335 AA.
AC B1W019;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=(+)-caryolan-1-ol synthase;
DE EC=4.2.1.138;
DE AltName: Full=(+)-beta-caryophyllene synthase;
DE EC=4.2.3.89;
GN Name=gcoA; OrderedLocusNames=SGR_2079;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, REACTION STEREOCHEMISTRY,
RP BIOPHYSICOCHEMICAL PROPERTIES, GENE NAME, INDUCTION, DISRUPTION PHENOTYPE,
RP AND REACTION MECHANISM.
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=21693706; DOI=10.1074/jbc.m111.265652;
RA Nakano C., Horinouchi S., Ohnishi Y.;
RT "Characterization of a novel sesquiterpene cyclase involved in (+)-
RT caryolan-1-ol biosynthesis in Streptomyces griseus.";
RL J. Biol. Chem. 286:27980-27987(2011).
CC -!- FUNCTION: Sesquiterpene cyclase that first catalyzes the cyclization of
CC farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (+)-beta-
CC caryophyllene intermediate, and then its conversion to (+)-caryolan-1-
CC ol via a second cyclization and the addition of a water molecule.
CC {ECO:0000269|PubMed:21693706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:31815, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:63190, ChEBI:CHEBI:175763; EC=4.2.3.89;
CC Evidence={ECO:0000269|PubMed:21693706};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-(E)-beta-caryophyllene + H2O = (+)-caryolan-1-ol;
CC Xref=Rhea:RHEA:31795, ChEBI:CHEBI:15377, ChEBI:CHEBI:63190,
CC ChEBI:CHEBI:63196; EC=4.2.1.138;
CC Evidence={ECO:0000269|PubMed:21693706};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21693706};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21693706};
CC Note=Binds 3 Mg(2+) ions per subunit. To a lesser extent, can also use
CC Mn(2+) instead of Mg(2+). Cannot use Fe(2+), Co(2+), Zn(2+), Ni(2+), or
CC Cu(2+). {ECO:0000269|PubMed:21693706};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=95.6 nM for farnesyl diphosphate (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:21693706};
CC Note=kcat is 0.025 sec(-1) for (+)-caryolan-1-ol formation (at pH 7.5
CC and 30 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 7.5 for (+)-caryolan-1-ol synthesis.
CC {ECO:0000269|PubMed:21693706};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius for (+)-caryolan-1-ol
CC synthesis. {ECO:0000269|PubMed:21693706};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- INDUCTION: Expressed under the control of A-factor (2-isocapryloyl-3R-
CC hydroxymethyl-gamma-butyrolactone), in an AdpA-dependent manner.
CC {ECO:0000269|PubMed:21693706}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not produce (+)-
CC caryolan-1-ol. {ECO:0000269|PubMed:21693706}.
CC -!- MISCELLANEOUS: A study of the reaction mechanism indicates that (+)-
CC caryolan-1-ol is synthesized by a proton attack on the C-8/C-9 double
CC bond of (+)-beta-caryophyllene.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AP009493; BAG18908.1; -; Genomic_DNA.
DR AlphaFoldDB; B1W019; -.
DR SMR; B1W019; -.
DR STRING; 455632.SGR_2079; -.
DR EnsemblBacteria; BAG18908; BAG18908; SGR_2079.
DR KEGG; sgr:SGR_2079; -.
DR eggNOG; ENOG5033VJC; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR OMA; CNDICSF; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000001685; Chromosome.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IDA:UniProtKB.
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 Hydrolase; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..335
FT /note="(+)-caryolan-1-ol synthase"
FT /id="PRO_0000418814"
FT MOTIF 83..87
FT /note="DDXXD motif"
FT MOTIF 220..228
FT /note="NSE/DTE motif"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 37906 MW; 28EFFDF108D53353 CRC64;
MSQITLPAFH MPFQSAGCHP GLAETREAAW EWAAAEGLDL SVPARRKMIR TRPELWISLI
FPQATQAHLD LFCQWLFWAF LVDDEFDDGP AGRDPLMCER AIARLVDVFD GAAPNGPMER
ALAGLRDRTC RGRSPQWNRQ FRRDTAAWLW TYYAEAVERA AGQVPSRAEF AKHRRDSVAM
QPFLCLHEIT AGIDLPDSAR SLPAYIALRN AVTDHSGLCN DICSFEKEAA LGYEHNAVRL
IQRDRGSTLQ EAVDEAGIQL ARIAERVQRA ERELIEEIEA AGIDGPTRTA LERCVRDYRG
LVRGDFDYHA RAERYTRPDL VELDERDSLS RHFAA
