ID   PENE_STREX              Reviewed;         584 AA.
AC   E3VWK3;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Pentalenolactone D synthase;
DE            EC=1.14.13.170;
DE   AltName: Full=Pentalenolactone biosynthesis protein E;
GN   Name=penE;
OS   Streptomyces exfoliatus (Streptomyces hydrogenans).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UC5319;
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, AND PATHWAY.
RC   STRAIN=UC5319;
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; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
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; HQ292066; ADO85591.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWK3; -.
DR   SMR; E3VWK3; -.
DR   KEGG; ag:ADO85591; -.
DR   BioCyc; MetaCyc:MON-16844; -.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0102285; F:1-deoxy-11-oxopentalenate oxygenase activity; IEA:UniProtKB-EC.
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; -; 2.
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..584
FT                   /note="Pentalenolactone D synthase"
FT                   /id="PRO_0000422005"
FT   BINDING         55..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..78
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..98
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         486
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            371
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   584 AA;  65386 MW;  D7662CACC6BEA6DF CRC64;
     MREKYRQERD KRSVGRTYQF ARGDFSRYAR DPYTERQERE PLTDEVDVAV VGAGIGGLLT
     GAHLRKETGL ERIRLIDGAG DVGGTWYWNR FPGVRCDVES YIYMPLLEET GTIPREKYST
     GPEIFAHLQQ IAHRYDLYRD ALFQTTVTEL RWDEAAGRWL VSTDRGDLIR ARYVAMSIGL
     MHRPKLPGLP GLETFAGHSF HTSRWDFDYT GGDSTGGLTK LKDKKVGVIG TGSTTIQLAP
     HLAEWAEQLI LFQRTPAAVD VRGNRPTPPE WAAGLAPGWQ QRRMENFHAL TSGVPQDEDL
     VQDRWTQTTA KLAAAILPTG DTGGDPKERA LAAERADFLK MEELRARIDS VVTDPATAAA
     LKPYYRVYCK RPCFHDGYLQ TFNRPNVTLV DTQGQGVERL TPAGVVANGR EYPLDCLIFA
     TGYEHEFAVP YTERAGYDIV GRDGLRLSEK WADGARTLHG LQVNGFPNCF ILSKVQAGRH
     VNIAYMLGEQ TRHLAHIVKC VEERGHQVVE ASEAGEKEWV EEILRLATND IDFLENCTPG
     LYNNEGDPSG LPLLNSSYGG GSVEFVNILR RWREAGDLAG LELR