IAFRS_STRV4
ID IAFRS_STRV4 Reviewed; 384 AA.
AC G2P5T1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Isoafricanol synthase {ECO:0000303|PubMed:24626486};
DE EC=4.2.3.157 {ECO:0000269|PubMed:24626486};
GN ORFNames=Strvi_5748 {ECO:0000312|EMBL:AEM85259.1};
OS Streptomyces violaceusniger (strain Tu 4113).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=653045;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu 4133;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ivanova N., Daligault H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hagen A., Katz L.,
RA Fiedler H.-P., Keasling J., Fortman J., Woyke T.;
RT "Complete sequence of chromosome of Streptomyces violaceusniger Tu 4113.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24626486; DOI=10.1039/c4cc00177j;
RA Riclea R., Citron C.A., Rinkel J., Dickschat J.S.;
RT "Identification of isoafricanol and its terpene cyclase in Streptomyces
RT violaceusniger using CLSA-NMR.";
RL Chem. Commun. (Camb.) 50:4228-4230(2014).
CC -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC isoafricanol. {ECO:0000269|PubMed:24626486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-isoafricanol +
CC diphosphate; Xref=Rhea:RHEA:53616, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:137522, ChEBI:CHEBI:175763;
CC EC=4.2.3.157; Evidence={ECO:0000269|PubMed:24626486};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5GMG2};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5GMG2};
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CP002994; AEM85259.1; -; Genomic_DNA.
DR AlphaFoldDB; G2P5T1; -.
DR SMR; G2P5T1; -.
DR STRING; 653045.Strvi_5748; -.
DR EnsemblBacteria; AEM85259; AEM85259; Strvi_5748.
DR KEGG; svl:Strvi_5748; -.
DR eggNOG; ENOG502Z881; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR BRENDA; 4.2.3.157; 15064.
DR Proteomes; UP000008703; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..384
FT /note="Isoafricanol synthase"
FT /id="PRO_0000449806"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
SQ SEQUENCE 384 AA; 42360 MW; 2C5878A98067A959 CRC64;
MHAHASRPQA RQTTLLRRAA LFDFPASADL SPGTEAARHH TIQWLSRFGV FEGHESVAEY
DALRFDVLAG LFYPRATGAD LNLGSDLVGW YFVFDDQFDG ELGSRPEAVA RLVADVIRIT
EEDTAHGRAQ DGEGPLLESF RDLWRRISSG RPQVWRDRFR HHWLEYLHSY HREALERTGA
LPGAGGDAPR SVEAVLALRR HSIGVQPCLD LNEPFGGYTL PPALHGGFPM ARMREATDDV
VVFTNDIASL DKELAVGDVH NSVIVQWERA GGELEDAVRH IADLANARYR WFEETAARLP
ALLTEAGADP GTHHAVGRYV DGMRHVMTGN LGWSVRTARY DERGTEAVSG GRQRPWAQLT
GAEELIRAGR GAPLPPLGSG SGSR