EREMS_SORC5
ID EREMS_SORC5 Reviewed; 329 AA.
AC A9FZ87;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=(+)-eremophilene synthase {ECO:0000303|PubMed:25504914};
DE EC=4.2.3.164 {ECO:0000269|PubMed:25504914};
DE AltName: Full=Sesquiterpene cyclase {ECO:0000303|PubMed:25504914};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:25504914};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:25504914};
GN Name=geoA {ECO:0000303|PubMed:25504914};
GN OrderedLocusNames=sce8552 {ECO:0000312|EMBL:CAN98722.1};
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 {ECO:0000312|Proteomes:UP000002139};
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, AND PATHWAY.
RC STRAIN=So ce56;
RX PubMed=25504914; DOI=10.1002/cbic.201402443;
RA Schifrin A., Ly T.T., Guennewich N., Zapp J., Thiel V., Schulz S.,
RA Hannemann F., Khatri Y., Bernhardt R.;
RT "Characterization of the gene cluster CYP264B1-geoA from Sorangium
RT cellulosum So ce56: biosynthesis of (+)-eremophilene and its
RT hydroxylation.";
RL ChemBioChem 16:337-344(2015).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield the bicyclic sesquiterpene eremophilene via a 1,10-
CC cyclization, which requires the abstraction of the pyrophosphate from
CC FPP to yield the (E,E)-germacradienyl cation. The only accepted
CC substrate is farnesyl diphosphate (FPP). {ECO:0000269|PubMed:25504914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-eremophilene + diphosphate;
CC Xref=Rhea:RHEA:52804, ChEBI:CHEBI:33019, ChEBI:CHEBI:137562,
CC ChEBI:CHEBI:175763; EC=4.2.3.164;
CC Evidence={ECO:0000269|PubMed:25504914};
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:25504914}.
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:25504914}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AM746676; CAN98722.1; -; Genomic_DNA.
DR RefSeq; WP_012241161.1; NC_010162.1.
DR AlphaFoldDB; A9FZ87; -.
DR SMR; A9FZ87; -.
DR STRING; 448385.sce8552; -.
DR EnsemblBacteria; CAN98722; CAN98722; sce8552.
DR KEGG; scl:sce8552; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_2_7; -.
DR OMA; DLIEYAM; -.
DR OrthoDB; 1869158at2; -.
DR BioCyc; SCEL448385:SCE_RS43810-MON; -.
DR BRENDA; 4.2.3.164; 9327.
DR UniPathway; UPA00213; -.
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 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..329
FT /note="(+)-eremophilene synthase"
FT /id="PRO_0000443303"
FT MOTIF 91..95
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:25504914"
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 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 317..318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 329 AA; 38073 MW; AE2338989D3053D0 CRC64;
MSSDRTSVVV SKRDAGGFEY PFAASCHPGR EVTEQRTLAW VRRLRLVPDG RSLSRLKATN
FSHLAAWLLP SASTQTLQLA SDFTAVLFLL DDAYDEGQLS TDPESVEWLN EKYLGELFGY
TEADMSDPLT RGMLDVRERI RRSHPHFFLN RWLSHFQYYY EANLWEANNR KQMRVPHLEE
YLMMRRYSGA VYTYCDLLEL LLERPLPLEV VQHPLIQTVR DICNDILCWT NDYFSLGKEL
TNGETHNLIV VLRNECVSTL EEAIDRLKDM HDRRVAEYQG VKEKVLALWA DDEIRLYLDA
VEAMIAGNQR WALEAGRYSG LESLIVRAG
