ID   LSD18_STRLS             Reviewed;         472 AA.
AC   B5M9L6;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Putative epoxidase LasC;
DE            EC=1.14.13.-;
DE   AltName: Full=Lasalocid biosynthesis protein Lsd18;
GN   Name=lsd18; Synonyms=lasC;
OS   Streptomyces lasalocidi (Streptomyces lasaliensis).
OG   Plasmid pKSL.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=324833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN LASALOCID BIOSYNTHESIS, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35851 / NRRL 3382R;
RX   PubMed=19025863; DOI=10.1002/cbic.200800585;
RA   Smith L., Hong H., Spencer J.B., Leadlay P.F.;
RT   "Analysis of specific mutants in the lasalocid gene cluster: evidence for
RT   enzymatic catalysis of a disfavoured polyether ring closure.";
RL   ChemBioChem 9:2967-2975(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35851 / NRRL 3382R; PLASMID=pKSL;
RX   PubMed=19129623; DOI=10.1271/bbb.80631;
RA   Migita A., Watanabe M., Hirose Y., Watanabe K., Tokiwano T., Kinashi H.,
RA   Oikawa H.;
RT   "Identification of a gene cluster of polyether antibiotic lasalocid from
RT   Streptomyces lasaliensis.";
RL   Biosci. Biotechnol. Biochem. 73:169-176(2009).
CC   -!- FUNCTION: May catalyze the stereoselective double epoxidation reaction
CC       leading to bisepoxyprelasalocid A, a bisepoxide intermediate in the
CC       biosynthesis of the polyether antibiotic lasalocid A.
CC       {ECO:0000269|PubMed:19025863}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- DISRUPTION PHENOTYPE: Deletion of this gene abolishes production both
CC       of lasalocid and of the minor cometabolite iso-lasalocid without
CC       leading to accumulation of an identifiable intermediate.
CC       {ECO:0000269|PubMed:19025863}.
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DR   EMBL; FM173265; CAQ64694.1; -; Genomic_DNA.
DR   EMBL; AB449340; BAG85033.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5M9L6; -.
DR   PRIDE; B5M9L6; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; FAD; Flavoprotein; Monooxygenase; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..472
FT                   /note="Putative epoxidase LasC"
FT                   /id="PRO_0000417071"
SQ   SEQUENCE   472 AA;  50490 MW;  695E8D1036E5C296 CRC64;
     MTNTRSAVVL GGGMAGMLVS SMLARHVGSV TVIDRDAFPA GPDLRKGVPQ ARHAHILWSG
     GARIVEELLP GTTDRLLGAG AHRIGIPDGQ VSYTAYGWQH RFPEAQFMIA CSRALLDWTV
     REETLREERI ALVEKTEVLA LLGDAGRVTG VRVRDQESGE EREVPADLVV DTTGRGSPSK
     RLLAELGLPA PEEEFVDSGM VYATRLFRAP EAAATNFPLV SVHADHRAGR PGCNAVLMPI
     EDGRWIVTVS GTRGGEPPAD DEGFARFARD GVRHPLVGEL IAKAQPLTSV ERSRSTVNRR
     LHYDRLATWP EGLVVLGDAV AAFNPVYGHG MSAAAHSVLA LRSQLGQRAF QPGLARAAQR
     AIAVAVDDAW VLATSHDIGY PGCRTQTRDP RLTRHAGERQ RVTDLVGLTA TRNQVVNRAA
     VALNTLSAGM ASMQDPAVMA AVRRGPEVPA PTEPPLRPDE VARLVSGAGV TA