ID   PNTD_STRAE              Reviewed;         299 AA.
AC   E3VWI8;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Pentalenolactone F synthase;
DE            EC=1.14.11.36;
DE   AltName: Full=Pentalenolactone biosynthesis protein D;
GN   Name=pntD;
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, PATHWAY, AND DISRUPTION PHENOTYPE.
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 Fe(2+) and alpha-ketoglutarate-dependent
CC       oxidation of pentalenolactone D to pentalenolactone F in the
CC       biosynthesis of pentalenolactone antibiotic. Also able to catalyze the
CC       oxidation of pentalenolactone D to pentalenolactone E.
CC       {ECO:0000269|PubMed:21250661}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + 2 O2 + pentalenolactone D = 2 CO2 + H2O +
CC         pentalenolactone F + 2 succinate; Xref=Rhea:RHEA:34579,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:70787,
CC         ChEBI:CHEBI:70789; EC=1.14.11.36;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by ascorbate. {ECO:0000250}.
CC   -!- PATHWAY: Antibiotic biosynthesis; pentalenolactone biosynthesis.
CC       {ECO:0000269|PubMed:21250661}.
CC   -!- DISRUPTION PHENOTYPE: Accumulation of pentalenolactone D and lack of
CC       production of pentalenolactone as well as the precursors
CC       pentalenolactones E and F. {ECO:0000269|PubMed:21250661}.
CC   -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR   EMBL; HQ292065; ADO85576.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWI8; -.
DR   SMR; E3VWI8; -.
DR   BRENDA; 1.14.11.36; 5975.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901780; P:pentalenolactone biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Vitamin C.
FT   CHAIN           1..299
FT                   /note="Pentalenolactone F synthase"
FT                   /id="PRO_0000422007"
FT   BINDING         105
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   299 AA;  33460 MW;  B0DD11B9F3851F72 CRC64;
     MEVTPIPGAP LGAVVHGARV TGDMDKTHLE EIWSALDTYL VLVLRGHETP SYEEFLAFGR
     RFGHIPKTGL TSGAHPEHNE ILIVSNLVED GRKIGVGDAE WMGWHTDYSF RPRVSQVGFL
     EAVEVPYSGG GETLFTDMYA LYESLSPEER RRLHSFRVRH ALRTGYEETI EEELQREVTL
     GEGADRIQPE DGTSTVHPLI ARNPRTGRRS VYISTLNTER IVDLAPDDSR ELLDGLLAHA
     GKPQYTYAHT WQPGDLVVWD QLGTVHAKQA FDPAERRVMR QVVSIFDDPA GPWRAEAAA