ID   PNTE_STRAE              Reviewed;         589 AA.
AC   E3VWI7;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Pentalenolactone D synthase;
DE            EC=1.14.13.170;
DE   AltName: Full=Pentalenolactone biosynthesis protein E;
GN   Name=pntE;
OS   Streptomyces arenae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=29301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu469;
RX   PubMed=21284395; DOI=10.1021/ja111279h;
RA   Zhu D., Seo M.J., Ikeda H., Cane D.E.;
RT   "Genome mining in streptomyces. Discovery of an unprecedented P450-
RT   catalyzed oxidative rearrangement that is the final step in the
RT   biosynthesis of pentalenolactone.";
RL   J. Am. Chem. Soc. 133:2128-2131(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR.
RC   STRAIN=Tu469;
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 pentalenolactone D in the biosynthesis
CC       of pentalenolactone antibiotic. {ECO:0000269|PubMed:21250661}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-11-oxopentalenate + H(+) + NADPH + O2 = H2O + NADP(+)
CC         + pentalenolactone D; Xref=Rhea:RHEA:34635, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:70780, ChEBI:CHEBI:70787;
CC         EC=1.14.13.170; Evidence={ECO:0000269|PubMed:21250661};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:21250661};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:21250661};
CC   -!- PATHWAY: Antibiotic biosynthesis; pentalenolactone biosynthesis.
CC       {ECO:0000269|PubMed:21250661}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; HQ292065; ADO85575.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWI7; -.
DR   SMR; E3VWI7; -.
DR   KEGG; ag:ADO85575; -.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0102285; F:1-deoxy-11-oxopentalenate oxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
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; IEA:UniProtKB-KW.
DR   GO; GO:1901780; P:pentalenolactone biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..589
FT                   /note="Pentalenolactone D synthase"
FT                   /id="PRO_0000422004"
FT   BINDING         60..61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         82..83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         90..91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            376
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   589 AA;  65853 MW;  0FC902CE15085BC7 CRC64;
     MDLEAVREKY RQERDKRGVG RTYQFARGDF SRYARDPYTE RREREPLTDE VDVAVVGAGI
     GGLLTGARLR EETGLERIRL IDEAGDVGGT WYWNRFPGVR CDVESYVYMP LLEEIGTIPT
     EKYSTGPEIF AHLQRIAHRY GLYRDALFQT TVTELRWDEA AARWLVSTDR GDLFRARYVA
     MSIGLMHRPK LPGLPGLETF AGHSFHTSRW DFGYTGGDST GGLTGLKDKR VGVIGTGSTT
     VQLAPHLAEW AERLYIFQRT PAAVDVRGNR PTPPGWADGL DAGWQQRRME NFHALTSGIP
     QDEDLVQDRW TQTTAELATA ILPTGDTGGD PKERALAAER ADFRKMEELR ARIDSVVTDP
     ATAAALKPYY RVYCKRPCFH DGYLQTFNRP NVTLVDTQGQ GVERLTASGV VANGREYPVD
     CLIFATGYEH EFAVPYTERA GYDIVGRGGV RLSEKWAQGA HTLHGLQVHG FPNCFILSKV
     QAGRHVNIAY MLGEQTRHLA HIVKCVEERG HRVVEASEAG EKEWVEEILR LASGDLDFLE
     NCTPGLYNNE GDPGGLPLLN SSYGGGSVEF VNILRRWREA GDLAGLELR