PEND_STREX
ID PEND_STREX Reviewed; 298 AA.
AC E3VWK4;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Pentalenolactone F synthase;
DE EC=1.14.11.36;
DE AltName: Full=Pentalenolactone biosynthesis protein D;
GN Name=penD;
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, PATHWAY, AND DISRUPTION PHENOTYPE.
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 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; HQ292066; ADO85592.1; -; Genomic_DNA.
DR AlphaFoldDB; E3VWK4; -.
DR SMR; E3VWK4; -.
DR BioCyc; MetaCyc:MON-16845; -.
DR BRENDA; 1.14.11.36; 6010.
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..298
FT /note="Pentalenolactone F synthase"
FT /id="PRO_0000422008"
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 132
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33368 MW; 6F98AA299076978E CRC64;
MDVTPIPGAA LGAVVHGAHV TGDMDKTQFE EIWAALDAHL VLVFRGHRTP SYEEFLAFGR
RFGYIPKTGL TSGAHPDHNE ILIVSNLVED GRKIGVGDAE WMGWHTDYSF RPRVSQVGFL
EAVEVPSCGG ETLFTDMYAL YESLSPEERK RMHSYRVRHA MRTGYEETIE EKLQREVSLG
GSGEQILPED GTSTIHPLIA RNPRTGRQSV YISTLNTERI VDLAPDDSRK LLDELLSHAG
KPEHTYAHTW QPGDIVMWDQ LGTVHAKQAF DPAELRVMRQ VVSIFDDPTD PWHAEVAA