AAMS_STRVT
ID AAMS_STRVT Reviewed; 338 AA.
AC D9XDR8;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=(-)-alpha-amorphene synthase ((2E,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:23307484};
DE EC=4.2.3.162 {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27666571, ECO:0000269|PubMed:27829890};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:23307484};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:23307484};
GN ORFNames=SSQG_00965 {ECO:0000312|EMBL:EFL30447.1};
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, AND REACTION MECHANISM.
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
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 [4]
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 sesquiterpene (1R,6S,7S)-(-)-alpha-
CC amorphene via a probable 1,6-cyclization, which could involve the
CC abstraction of the pyrophosphate from FPP to yield a (R)-bisabolyl
CC cation (PubMed:23307484, PubMed:27666571, PubMed:27829890). The only
CC accepted substrate is (2E,6E)-farnesyl diphosphate (FPP)
CC (PubMed:27829890). {ECO:0000269|PubMed:23307484,
CC ECO:0000269|PubMed:27666571, ECO:0000269|PubMed:27829890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-alpha-amorphene +
CC diphosphate; Xref=Rhea:RHEA:53640, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:137533, ChEBI:CHEBI:175763; EC=4.2.3.162;
CC Evidence={ECO:0000269|PubMed:23307484, 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-Glu (DDXXE) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG657757; EFL30447.1; -; Genomic_DNA.
DR AlphaFoldDB; D9XDR8; -.
DR SMR; D9XDR8; -.
DR STRING; 591159.ACEZ01000042_gene1853; -.
DR EnsemblBacteria; EFL30447; EFL30447; SSQG_00965.
DR HOGENOM; CLU_042538_4_2_11; -.
DR BRENDA; 4.2.3.162; 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 SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..338
FT /note="(-)-alpha-amorphene synthase ((2E,6E)-farnesyl
FT diphosphate cyclizing)"
FT /id="PRO_0000443240"
FT MOTIF 105..109
FT /note="DDXXE motif"
FT /evidence="ECO:0000305|PubMed:27829890"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 327..328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 102
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 106
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 177
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 338 AA; 37003 MW; 21A6A7BBDFC98398 CRC64;
MAKMSTTHEE IALAGPDGIP AVDLRDLIDA QLYMPFPFER NPHASEAAAG VDHWLSTWGL
TDDPAVAAMI SCTRPAELAA FNGPDMDSGL LQIAANQIAY QFVFDDRAED IGRHSPGRLL
PMLSESVAIL RDGQPPTTPL GAALADLHRQ VQERCTPAQA ARWAWNSREY VHGLLYEAVA
QAHPAPVESG LCRSIRSLIA GVEPFYPLCE AAQRCELAPE ELHHPAMRRL SRLSADAAVW
IPDLFSAVKE QRAGGMINLA LAYRRTHRCS LPAAVTLAVR HINSTIREFE DLYGEVRPEL
SPSGIGYVEG MAGWIRGCYF WSRTVPRYAD TLTAPAGL
