PNTM_STRAE
ID PNTM_STRAE Reviewed; 398 AA.
AC E3VWI3;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Pentalenolactone synthase;
DE EC=1.14.19.8;
DE AltName: Full=Pentalenolactone biosynthesis protein M;
GN Name=pntM;
OS Streptomyces arenae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=29301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
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).
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=430 uM for pentalenolactone F {ECO:0000269|PubMed:21284395};
CC Note=kcat is 8.8 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; HQ292065; ADO85571.1; -; Genomic_DNA.
DR PDB; 5L1O; X-ray; 2.03 A; A=1-398.
DR PDB; 5L1P; X-ray; 2.28 A; A=1-398.
DR PDB; 5L1Q; X-ray; 2.03 A; A=1-398.
DR PDB; 5L1R; X-ray; 2.00 A; A=1-398.
DR PDB; 5L1S; X-ray; 2.08 A; A=1-398.
DR PDB; 5L1T; X-ray; 2.08 A; A=1-398.
DR PDB; 5L1U; X-ray; 2.07 A; A=1-398.
DR PDB; 5L1V; X-ray; 2.12 A; A=1-398.
DR PDB; 5L1W; X-ray; 2.06 A; A=1-398.
DR PDBsum; 5L1O; -.
DR PDBsum; 5L1P; -.
DR PDBsum; 5L1Q; -.
DR PDBsum; 5L1R; -.
DR PDBsum; 5L1S; -.
DR PDBsum; 5L1T; -.
DR PDBsum; 5L1U; -.
DR PDBsum; 5L1V; -.
DR PDBsum; 5L1W; -.
DR AlphaFoldDB; E3VWI3; -.
DR SMR; E3VWI3; -.
DR KEGG; ag:ADO85571; -.
DR BRENDA; 1.14.19.8; 5975.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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 3D-structure; Antibiotic biosynthesis; Heme; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1..398
FT /note="Pentalenolactone synthase"
FT /id="PRO_0000422010"
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"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5L1R"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 106..129
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:5L1R"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 176..199
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:5L1R"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 350..367
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:5L1R"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:5L1R"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5L1R"
SQ SEQUENCE 398 AA; 44164 MW; 06DB17430F6ABBD0 CRC64;
MTDLPRLPFD NPDIMGIAPQ MLALQKEGPI ARVGTAGEDA WLVTRYDEVR TLLADRRLRL
SNPNPQPSAK SAARAFMVAL MAGDDHETEP ARHAQMRSLL IPRFSTRRLR LMKTRIEHHV
DELLDQLAAS APPVDLHRVL SFRLPTMVVC DLLGVPLADR ERFGQWARGT FDQSDNEHSA
NTFQQVVDYM LELVARKRVE PGDDILSELI AEKDGALSDA DIAHLGNAVL LFGYETTIVR
IDLGTLLLLR NPVQRAQLAE DPGLAPAAVE EILRLGVGGK GSNALIPRYA HGDITVGETV
IRTGDAVMLA IGAANYDDRA FPDGGLFDLT RVRPRSHLAF GHGARHCIGR TLARIELTAV
FERLFRRLPD LRLAVPEESL RWQEHRITGG FDEIPVTF
