GERS_STRFA
ID GERS_STRFA Reviewed; 356 AA.
AC E8W6C7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=(+)-(1(10)E,4E,6S,7R)-germacradien-6-ol synthase {ECO:0000303|PubMed:26361082};
DE EC=4.2.3.166 {ECO:0000269|PubMed:26361082};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:26361082};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:26361082};
GN OrderedLocusNames=Sfla_1617 {ECO:0000312|EMBL:ADW03055.1};
OS Streptomyces pratensis (strain ATCC 33331 / IAF-45CD).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=591167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33331 / IAF-45CD;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Brumm P., Mead D.,
RA Woyke T.;
RT "Complete sequence of chromosome of Streptomyces flavogriseus ATCC 33331.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND DOMAIN.
RC STRAIN=ATCC 33331 / IAF-45CD;
RX PubMed=26361082; DOI=10.1002/anie.201507615;
RA Rabe P., Barra L., Rinkel J., Riclea R., Citron C.A., Klapschinski T.A.,
RA Janusko A., Dickschat J.S.;
RT "Conformational analysis, thermal rearrangement, and EI-MS fragmentation
RT mechanism of (1(10)E,4E,6S,7R)-germacradien-6-ol by (13)C-labeling
RT experiments.";
RL Angew. Chem. Int. Ed. 54:13448-13451(2015).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield the sesquiterpene (+)-(1(10)E,4E,6S,7R)-germacradien-6-
CC ol via a putative 1,10-cyclization, which could require the abstraction
CC of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cation.
CC The only accepted substrate is farnesyl diphosphate (FPP).
CC {ECO:0000269|PubMed:26361082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-(1(10)E,4E,6S,7R)-
CC germacradien-6-ol + diphosphate; Xref=Rhea:RHEA:12192,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:137564,
CC ChEBI:CHEBI:175763; EC=4.2.3.166;
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}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Xaa-Asp (DDXXXD) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:26361082}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CP002475; ADW03055.1; -; Genomic_DNA.
DR RefSeq; WP_014153723.1; NC_016114.1.
DR AlphaFoldDB; E8W6C7; -.
DR SMR; E8W6C7; -.
DR STRING; 591167.Sfla_1617; -.
DR EnsemblBacteria; ADW03055; ADW03055; Sfla_1617.
DR KEGG; sfa:Sfla_1617; -.
DR PATRIC; fig|591167.6.peg.1658; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_2_11; -.
DR OMA; LCDWGNW; -.
DR OrthoDB; 1869158at2; -.
DR BRENDA; 4.2.3.166; 15070.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000002066; 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.
FT CHAIN 1..356
FT /note="(+)-(1(10)E,4E,6S,7R)-germacradien-6-ol synthase"
FT /id="PRO_0000443322"
FT MOTIF 86..91
FT /note="DDXXXD motif"
FT /evidence="ECO:0000305|PubMed:26361082"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
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 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 181
FT /ligand="substrate"
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 231
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="substrate"
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 314..315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 356 AA; 40241 MW; 2EB4B1C61F7D9019 CRC64;
MTSQASAPKI PQLWVPLPSG IHPSWREIDQ GSAAWLDRFG LYSDHAQRER LTRISVGEIT
GRGGPDGRLA ALQWTADFLM WLFAFDDEYC DEGPAAASPD ATLLIITKLQ RIVEVPWAAP
ADDNYSAALL ELRLRLDDLT TPVQTARWAA SFRAYLQGQI WMAANSTYGR IPTLSDHLAV
RLDSSGVKIF STLSEIIHGY DLPAADYDRH DVRGFVEVFA AIIGWSNDLV SYHKERRRSQ
DSYGNVVDLI AHERQCSVEE AVSETATMHT RAMALYLRLR DQILRDAEPE LRKWITDCDS
WIRADYDWSL TTHRYVNPDD PADLPVGSAE APFRAREADQ PLPIASVSWW WTLLKD
