PTLE_STRAW
ID PTLE_STRAW Reviewed; 594 AA.
AC Q82IY8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Neopentalenolactone D synthase;
DE EC=1.14.13.171;
DE AltName: Full=Neopentalenolactone biosynthesis protein E;
GN Name=ptlE; OrderedLocusNames=SAV_2994;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=21250661; DOI=10.1021/bi1019786;
RA Seo M.J., Zhu D., Endo S., Ikeda H., Cane D.E.;
RT "Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger
RT monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the
RT final steps of the biosynthesis of pentalenolactone and
RT neopentalenolactone.";
RL Biochemistry 50:1739-1754(2011).
CC -!- FUNCTION: Catalyzes the flavin-dependent Baeyer-Villiger oxidation of
CC 1-deoxy-11-oxopentalenic acid to neopentalenolactone D in the
CC biosynthesis of neopentalenolactone antibiotic.
CC {ECO:0000269|PubMed:21250661}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-11-oxopentalenate + H(+) + NADPH + O2 = H2O + NADP(+)
CC + neopentalenolactone D; Xref=Rhea:RHEA:34639, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:70780, ChEBI:CHEBI:70859;
CC EC=1.14.13.171; Evidence={ECO:0000269|PubMed:21250661};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- PATHWAY: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
CC {ECO:0000269|PubMed:21250661}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both ptlE and ptlD accumulate 1-
CC deoxy-11-oxopentalenic acid. {ECO:0000269|PubMed:21250661}.
CC -!- MISCELLANEOUS: S.avermitilis does not produce pentalenolactone itself
CC in vivo but instead a group of new metabolites that are
CC neopentalenolactone derivatives. {ECO:0000305|PubMed:21250661}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BA000030; BAC70705.1; -; Genomic_DNA.
DR RefSeq; WP_010984425.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82IY8; -.
DR SMR; Q82IY8; -.
DR STRING; 227882.SAV_2994; -.
DR EnsemblBacteria; BAC70705; BAC70705; SAVERM_2994.
DR KEGG; sma:SAVERM_2994; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006937_8_2_11; -.
DR OMA; PWYPTWC; -.
DR OrthoDB; 630753at2; -.
DR BioCyc; MetaCyc:MONMETA-16851; -.
DR UniPathway; UPA01021; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901336; P:lactone biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..594
FT /note="Neopentalenolactone D synthase"
FT /id="PRO_0000422003"
FT BINDING 64..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 86..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 94..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 106..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 379
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 594 AA; 65925 MW; 1DDC6A3EC9BFE02A CRC64;
MVDIEAVRAK YREERDKRVQ ADGGRQYLSA QGEFAHYADD PHAKPIERAP VSDEVDVTII
GAGIGGLLLG ARLREACAFD TIRLVDKAGD VGGTWYWNRF PGLRCDVESY VYMPLLEELG
RLPSEKYATG AEIFEHCQAI ARTYDLYDEA LLQTSVTELS WDEDSSRWLV RTDRGDLVRS
RFVAMAIGSL HRPKLPSIPG TEAFQGHSFH TSRWDFAYTG GDISGGLEKL GDKRVGIVGT
GATAVQCIPH LAESAAHLYV FQRTPSTVSV RNNRPTDPGW AAGLEPGWQQ RRMDNFHALT
SGVDQDVDLV QDGWTEITSK LAAILPKSAA DADPKDIGTA VELADFHKME ELRKRVDAIV
HDKDTADALK PYYRLFCKRP CFHDGYLDTY NRPNVTLVDT QGRGVERLTP TSVVAGGREY
PVDCLIFASG YESEFGVPYT NRTGFSIVGR DGIRLSEKWA EGARTFHGLQ VNGFPNCFIL
SKAQSGLHVN VPYMLNEQSK HVAYILKAVQ QRGRQVVEAS ATGEKEWVET ILRLANRNLD
FTESCTPGLF NNEGNPRNVA ILNSSYGGGS VGFVNILKRW READDLADLE LREG
