ECUB_STRRD
ID ECUB_STRRD Reviewed; 330 AA.
AC D2B747;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=4-epi-cubebol synthase ((2E,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:27829890};
DE EC=4.2.3.170 {ECO:0000269|PubMed:27666571, ECO:0000269|PubMed:27829890};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:27829890};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:27829890};
GN OrderedLocusNames=Sros_6866 {ECO:0000312|EMBL:ACZ89572.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC Streptosporangium.
OX NCBI_TaxID=479432;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000312|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
RX PubMed=27666571; DOI=10.1002/anie.201608042;
RA Rinkel J., Rabe P., Garbeva P., Dickschat J.S.;
RT "Lessons from 1,3-hydride shifts in sesquiterpene cyclizations.";
RL Angew. Chem. Int. Ed. 55:13593-13596(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, AND PATHWAY.
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
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 sesquiterpenol 4-epi-cubebol via a 1,10-
CC cyclization, which requires the abstraction of the pyrophosphate from
CC FPP to yield a (E,E)-germacradienyl cation (PubMed:27666571,
CC PubMed:27829890). The only accepted substrate is (2E,6E)-farnesyl
CC diphosphate (FPP) (PubMed:27829890). {ECO:0000269|PubMed:27666571,
CC ECO:0000269|PubMed:27829890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = 4-epi-cubebol +
CC diphosphate; Xref=Rhea:RHEA:54048, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138041, ChEBI:CHEBI:175763;
CC EC=4.2.3.170; Evidence={ECO:0000269|PubMed:27666571,
CC 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-Xaa-Glu (DDXXXE) 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; CP001814; ACZ89572.1; -; Genomic_DNA.
DR AlphaFoldDB; D2B747; -.
DR SMR; D2B747; -.
DR STRING; 479432.Sros_6866; -.
DR EnsemblBacteria; ACZ89572; ACZ89572; Sros_6866.
DR KEGG; sro:Sros_6866; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_2_11; -.
DR OMA; LCDWGNW; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000002029; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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..330
FT /note="4-epi-cubebol synthase ((2E,6E)-farnesyl diphosphate
FT cyclizing)"
FT /id="PRO_0000443245"
FT MOTIF 91..96
FT /note="DDXXXE motif"
FT /evidence="ECO:0000305|PubMed:27829890"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 316..317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 88
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 92
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 165
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 188
FT /note="Plays a critical role for abstraction of the
FT pyrophosphate group"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 330 AA; 37807 MW; 38C734520017CCAE CRC64;
MGTTTTHKFD RPLRLPPLPC PFPSEVNPYV EQVDKETLEW LIDSEMLDDA ETVERYRQAK
YGWLSARTYP YAEHHTLRLV SDWCVWLFAF DDAFCESDRR AAEIARALPQ LYAVLEDLDV
GSEVDDVFAK SLLEIKGRIA AYGDDEQLDR WRNVTKDYLF AQVWEAANRE DEVVPSLEDY
IFMRRRTGAM LTVFALIDVA SGRSLSADEW RHPGMRAITE SANDVVVWDN DLISYAKESN
SGNSRNNLVN VLAEHRHYSR QEAMEEIGEM RNQAIADMVA VRPSLEALGS DAVLAYVRGL
EFWISGSVDY SLTSSRYTDA WRTARQPSIR
