EAES_STRVT
ID EAES_STRVT Reviewed; 343 AA.
AC D9XD61;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=7-epi-alpha-eudesmol synthase ((2E,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:23307484};
DE EC=4.2.3.169 {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27829890};
DE AltName: Full=Terpene cyclase {ECO:0000303|PubMed:23307484};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:23307484};
GN ORFNames=SSQG_07226 {ECO:0000312|EMBL:EFL36708.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=591159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000312|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX PubMed=23307484; DOI=10.1002/anie.201209103;
RA Rabe P., Dickschat J.S.;
RT "Rapid chemical characterization of bacterial terpene synthases.";
RL Angew. Chem. Int. Ed. 52:1810-1812(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, AND PATHWAY.
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
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 7-epi-alpha-eudesmol via a
CC 1,10-cyclization, which requires the abstraction of the pyrophosphate
CC from FPP to yield the (E,E)-germacradienyl cation (PubMed:23307484,
CC PubMed:27829890). The only accepted substrate is (2E,6E)-farnesyl
CC diphosphate (FPP) (PubMed:27829890). {ECO:0000269|PubMed:23307484,
CC ECO:0000269|PubMed:27829890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = 7-epi-alpha-eudesmol +
CC diphosphate; Xref=Rhea:RHEA:54044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138040, ChEBI:CHEBI:175763;
CC EC=4.2.3.169; Evidence={ECO:0000269|PubMed:23307484,
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-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; GG657757; EFL36708.1; -; Genomic_DNA.
DR RefSeq; WP_003994861.1; NZ_GG657757.1.
DR AlphaFoldDB; D9XD61; -.
DR SMR; D9XD61; -.
DR STRING; 591159.ACEZ01000214_gene165; -.
DR EnsemblBacteria; EFL36708; EFL36708; SSQG_07226.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR OrthoDB; 1869158at2; -.
DR BRENDA; 4.2.3.169; 6116.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
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..343
FT /note="7-epi-alpha-eudesmol synthase ((2E,6E)-farnesyl
FT diphosphate cyclizing)"
FT /id="PRO_0000443241"
FT MOTIF 80..84
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27829890"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 230
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 317..318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 77
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 81
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 156
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 343 AA; 39255 MW; 1187FE43FBD2AEFC CRC64;
MPQDVRFDLP FETPVSKHLE SARARHLRWV WEMRLVHSRE GFEEYRSWDL PQAAARTYPH
ASADDMVVLM NWFSLAFLFD DQFDASRPDR ADRIAEVARE LIVTPLRPAG TPPRVACPIT
LAWTEVWKHL SHGMSLTWQS RFAASWGRFL EAHCEEVDLA ARGLEGTLGL VEFTEFRRRT
VGIHHSIDAG ERSRGFEVPA QAMAHPVMER MRDLAADTIG FMNDIHSFER EKRRGDGHNL
IAVLRRERGC SWQEATDEAY RMTIARLDEY LELQERVPQM CDELRLDEAQ RDGVRLGVEA
IQHWINGNYE WALTSGRYAA AKEGAVATAE LAGRGSVDDL LTV
