ID   IAFRS_STRMQ             Reviewed;         395 AA.
AC   A0A291SJC7;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Isoafricanol synthase {ECO:0000303|PubMed:28247907};
DE            EC=4.2.3.157 {ECO:0000269|PubMed:28247907};
GN   ORFNames=DNK48_39945 {ECO:0000312|EMBL:QDL74490.1},
GN   SMALA_0716 {ECO:0000312|EMBL:ATL80951.1};
OS   Streptomyces malaysiensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=92644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4137;
RA   Samborskyy M., Dickens S., Scott N., Haydock S., Leadlay P.;
RT   "Deciphering the complete genome sequence of Streptomyces malaysiensis
RT   DSM4137, an unusually prolific producer of assembly-line natural product
RT   antibiotics.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4137;
RA   Robison K.E.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 4137;
RX   PubMed=28247907; DOI=10.1039/c7ob00234c;
RA   Rabe P., Samborskyy M., Leadlay P.F., Dickschat J.S.;
RT   "Isoafricanol synthase from Streptomyces malaysiensis.";
RL   Org. Biomol. Chem. 15:2353-2358(2017).
CC   -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC       isoafricanol. {ECO:0000269|PubMed:28247907}.
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:28247907};
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; CP023992; ATL80951.1; -; Genomic_DNA.
DR   EMBL; CP029823; QDL74490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291SJC7; -.
DR   SMR; A0A291SJC7; -.
DR   EnsemblBacteria; ATL80951; ATL80951; SMALA_0716.
DR   KEGG; smal:SMALA_0716; -.
DR   Proteomes; UP000222153; Chromosome.
DR   Proteomes; UP000318530; 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..395
FT                   /note="Isoafricanol synthase"
FT                   /id="PRO_0000449805"
FT   REGION          346..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:B5GMG2"
SQ   SEQUENCE   395 AA;  43387 MW;  11DC8B3AC43A8AF9 CRC64;
     MHTHASRPHA RQSALPRRAA LFDFPASADL SPDTGAARQH TIQWLSRFRV FENHASVEEY
     DALRFDVLTG LFYPRATGAD LNLGSDLVGW YFVFDDQFDG ELGCRPEEVA RLVADVIRVT
     EEDMAPGGTG GGEGPLLESF RDLWHRINSG RPRVWRDRFR HHWLEYLHSY HREALERTGA
     APADGGGDAP RSVEDVLALR RHSIGVQPCL DLNEPFGGYT LPSALHGGFP LARMREATDD
     VVVFTNDIAS LDKELAVGDV HNSVIVQWKL AGGGVEDAVR HIAGLANARY GWFEETAARL
     PELLAEAGAD PGTHRAVGRY VDGMRHVMTG NLGWSLRTAR YDERGTEAVS GGRERPWARL
     TGAEDLIRAG RGAPPPPGSG PDTRQPMPSE PSQLA