PTLD_STRAW
ID PTLD_STRAW Reviewed; 306 AA.
AC Q82IY7;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pentalenolactone F synthase;
DE EC=1.14.11.36;
DE AltName: Full=Neopentalenolactone F synthase;
DE EC=1.14.11.-;
DE AltName: Full=Neopentalenolactone biosynthesis protein D;
GN Name=ptlD; OrderedLocusNames=SAV_2995;
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, COFACTOR, 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 Fe(2+) and alpha-ketoglutarate-dependent
CC oxidation of pentalenolactone D to pentalenolactone F. Also able to
CC catalyze the oxidation of pentalenolactone D to pentalenolactone E. In
CC presence of neopentalenolactone D, mediates production of PL308 and
CC possibly neopentalenolactone E. {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 Evidence={ECO:0000269|PubMed:21250661};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:21250661};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:21250661};
CC -!- ACTIVITY REGULATION: Activated by ascorbate. {ECO:0000250}.
CC -!- PATHWAY: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
CC {ECO:0000269|PubMed:21250661}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of pentalenolactone D.
CC {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 TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; BA000030; BAC70706.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82IY7; -.
DR SMR; Q82IY7; -.
DR STRING; 227882.SAV_2995; -.
DR EnsemblBacteria; BAC70706; BAC70706; SAVERM_2995.
DR KEGG; sma:SAVERM_2995; -.
DR eggNOG; COG2175; Bacteria.
DR HOGENOM; CLU_036005_2_0_11; -.
DR OMA; IHPVGAH; -.
DR BioCyc; MetaCyc:MONMETA-16852; -.
DR UniPathway; UPA01021; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901336; P:lactone 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 1: Evidence at protein level;
KW Antibiotic biosynthesis; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..306
FT /note="Pentalenolactone F synthase"
FT /id="PRO_0000422006"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 306 AA; 34236 MW; 2B65DC1A7D051670 CRC64;
MSRAMDITRI PGSAIGAVVA GADFSGTIDD TQVEEIWQAL DQHLVLVFRG HKDPSNDDLL
MFARRFGHVP KTGLTTGASP DHNEILLISN ILDENGQKIG VGNAEWMDWH TDYSFRPRVS
RIGFLAAVEL PPSGGGQTLF TDMYTAYESL PDDLRQRLHS YRARHSLRSG YEDVIEEEYQ
GEVSIEGPTA KPFVAPEDGT ATVHQLIARN PRTGRRAVYA NPLNTKRILE LDVTSSKEVL
QQLFAKPGEP ELTYAHEWLP GDIVMWDQLG TVHAKRAFDP TERRLLRKVV TIFDDPAEPW
HPEDAA
