ID   ECUBS_SORC5             Reviewed;         315 AA.
AC   A9GK58;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=10-epi-cubebol synthase {ECO:0000303|PubMed:26947062};
DE            EC=4.2.3.175 {ECO:0000269|PubMed:26947062};
GN   OrderedLocusNames=sce6369 {ECO:0000312|EMBL:CAN96536.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=So ce56;
RX   PubMed=26947062; DOI=10.1039/c6ob00130k;
RA   Schifrin A., Khatri Y., Kirsch P., Thiel V., Schulz S., Bernhardt R.;
RT   "A single terpene synthase is responsible for a wide variety of
RT   sesquiterpenes in Sorangium cellulosum Soce56.";
RL   Org. Biomol. Chem. 14:3385-3393(2016).
CC   -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC       10-epi-cubebol. Is also responsible for the formation of many other
CC       sesquiterpenes, mainly cadalanes and cubebanes, including 1,10-di-epi-
CC       cubebol and the cadalanes delta-cadinene, T-cadinol and alpha-cadinol.
CC       {ECO:0000269|PubMed:26947062}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = 10-epi-cubebol +
CC         diphosphate; Xref=Rhea:RHEA:54064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:138045, ChEBI:CHEBI:175763;
CC         EC=4.2.3.175; Evidence={ECO:0000269|PubMed:26947062};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:B5GMG2};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5GMG2};
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AM746676; CAN96536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9GK58; -.
DR   SMR; A9GK58; -.
DR   STRING; 448385.sce6369; -.
DR   EnsemblBacteria; CAN96536; CAN96536; sce6369.
DR   KEGG; scl:sce6369; -.
DR   eggNOG; COG0664; Bacteria.
DR   HOGENOM; CLU_042538_2_1_7; -.
DR   OMA; NHTLESA; -.
DR   BRENDA; 4.2.3.175; 9327.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..315
FT                   /note="10-epi-cubebol synthase"
FT                   /id="PRO_0000449804"
FT   MOTIF           79..83
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   MOTIF           220..228
FT                   /note="NXXXSXXXE motif"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
SQ   SEQUENCE   315 AA;  36142 MW;  C63F19BE4DAFA14C CRC64;
     MHRALLCPFP ATTPHPQAAQ LANDCLEWTR KCGLLPDESP RTLDKVRSYS ALAAHCYPDA
     HFERLRAICD YYSWLFFFDD VCENTSLNGA EPKVVSSLLF DVYGVLRGPT AAVGHAPFAQ
     ALADIWRRIG DGCPGFWRRR LIRHVENYID GCVWEAQNRQ LDRVPSRAVF EGMRMHTSTM
     YEFWDFIEYA GDLFLPDEVV EHPLVAEVRR AGNAIASFAN DIYSLRKETS NRDVHNLVVV
     LMHEERIELE AAYARAAGIH DAQVEHFLDL VKHLPTFSAT IDRNLARYVE GIRIWIRANH
     DWSIVTPRYN EPDAR