ID   PENM_STREX              Reviewed;         398 AA.
AC   E3VWJ9;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Pentalenolactone synthase;
DE            EC=1.14.19.8;
DE   AltName: Full=Pentalenolactone biosynthesis protein M;
GN   Name=penM;
OS   Streptomyces exfoliatus (Streptomyces hydrogenans).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
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).
CC   -!- FUNCTION: Catalyzes the final step in the biosynthesis of the
CC       sesquiterpenoid antibiotic pentalenolactone by mediating the oxidative
CC       rearrangement of pentalenolactone F to pentalenolactone.
CC       {ECO:0000269|PubMed:21284395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + O2 + pentalenolactone F + 2 reduced [2Fe-2S]-
CC         [ferredoxin] = 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin] +
CC         pentalenolactone; Xref=Rhea:RHEA:34575, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:70789, ChEBI:CHEBI:70790; EC=1.14.19.8;
CC         Evidence={ECO:0000269|PubMed:21284395};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:21284395};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=340 uM for pentalenolactone F {ECO:0000269|PubMed:21284395};
CC         Note=kcat is 10.5 min(-1) with pentalenolactone F as substrate.;
CC   -!- PATHWAY: Antibiotic biosynthesis; pentalenolactone biosynthesis.
CC       {ECO:0000269|PubMed:21284395}.
CC   -!- DISRUPTION PHENOTYPE: Accumulation of the precursor pentalenolactone F
CC       and lack of production of pentalenolactone.
CC       {ECO:0000269|PubMed:21284395}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; HQ292066; ADO85587.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWJ9; -.
DR   SMR; E3VWJ9; -.
DR   KEGG; ag:ADO85587; -.
DR   BioCyc; MetaCyc:MON-16836; -.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IDA:UniProtKB.
DR   GO; GO:1901780; P:pentalenolactone biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..398
FT                   /note="Pentalenolactone synthase"
FT                   /id="PRO_0000422011"
FT   BINDING         347
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  44396 MW;  B4C89089269538BA CRC64;
     MNELPRLPFD NPAILGIAPQ MRALQKEGPI VRVRTAGEDA WLITRYDEVK ALLSDRRLGL
     SDPKPERAAK STARITMMAL MAGDDYDREA TEHPQMRELL VPRFSTRRMR VMKARIEQHV
     DELLDQLAAS VAPVDLHRAL SFPLPTMVVC DLLGVPLADR ERIGQWARGT FDQSDSLHSV
     NTFQQVVDYM MELVQRKRTE PGDDILSELI AEKDGTLSDE YIAHLGCAVL LFGYETTIVR
     IDMGVLLMLR NPAQRALLAE NPALAPAAVE EILRLAVGGK GSNALIPRYA HSDITVGETV
     IRTGDAVMLA IGAANIDGHA FPHADLFDLS REKPKAHMAF GHGTRHCIGR VLARIELTAV
     FERLFRRLPN LQLAVPEESL RWQEHRITGG FDEIPVTF