TMUUS_ROSCS
ID TMUUS_ROSCS Reviewed; 326 AA.
AC A7NH01;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=(+)-T-muurolol synthase ((2E,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:23307484};
DE EC=4.2.3.98 {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27666571, 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 OrderedLocusNames=Rcas_0622 {ECO:0000312|EMBL:ABU56748.1};
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8 {ECO:0000312|Proteomes:UP000000263};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 13941 / HLO8;
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 13941 / HLO8;
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, DOMAIN, AND PATHWAY.
RC STRAIN=DSM 13941 / HLO8;
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) into (+)-T-muurolol via a 1,10-cyclization, which requires
CC isomerization of FPP to nerolidyl diphosphate (NPP) and then
CC abstraction of the pyrophosphate from intermediate NPP leading to a
CC (E,Z)-germacradienyl (helminthogermacradienyl) cation.
CC {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27666571,
CC ECO:0000269|PubMed:27829890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-T-muurolol +
CC diphosphate; Xref=Rhea:RHEA:32011, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63704, ChEBI:CHEBI:175763;
CC EC=4.2.3.98; Evidence={ECO:0000269|PubMed:23307484,
CC ECO:0000269|PubMed:27666571, 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; CP000804; ABU56748.1; -; Genomic_DNA.
DR RefSeq; WP_012119179.1; NC_009767.1.
DR AlphaFoldDB; A7NH01; -.
DR SMR; A7NH01; -.
DR STRING; 383372.Rcas_0622; -.
DR EnsemblBacteria; ABU56748; ABU56748; Rcas_0622.
DR KEGG; rca:Rcas_0622; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_2_0; -.
DR OMA; DLIEYAM; -.
DR OrthoDB; 1869158at2; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000263; 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..326
FT /note="(+)-T-muurolol synthase ((2E,6E)-farnesyl
FT diphosphate cyclizing)"
FT /id="PRO_0000443244"
FT MOTIF 81..85
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27829890"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 309..310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 78
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 82
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"
FT SITE 179
FT /note="Plays a critical role for abstraction of the
FT pyrophosphate group"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 326 AA; 37422 MW; 394840A09681FFD0 CRC64;
MDQDYRARLV YPFSGAISPH ADIVDQATLA WAAMFGLLTD SLRHKSRRLQ YGLLAARAYP
RADREMLQIA ADWIAWLFFM DDQCDETGIG RDLQRMIALH ERFLAILDGA TPEAHDCALT
YALADLRRRL ALRAPDNWLR RFSEHVRLYF TANRWETVNR QRGATPNVAT YCAARLFSGA
VYACFDLIEL AEQIELPFYA RHHSIVQQLE QAANNIICWC NDVLSYPKEM QHGDRHNLVL
VIQGEHQCSL PEAIDRALDL HAREVATFVR KRTCVPYFDA AVNTALEKYV TGLQFWICAN
RDWSLTATRY APTHKSQEMV MAVAQQ
