PTLI_STRAW
ID PTLI_STRAW Reviewed; 449 AA.
AC Q82IY3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Pentalenene oxygenase;
DE EC=1.14.15.32 {ECO:0000269|PubMed:17017767};
GN Name=ptlI; OrderedLocusNames=SAV_2999;
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=17017767; DOI=10.1021/ja0639214;
RA Quaderer R., Omura S., Ikeda H., Cane D.E.;
RT "Pentalenolactone biosynthesis. Molecular cloning and assignment of
RT biochemical function to PtlI, a cytochrome P450 of Streptomyces
RT avermitilis.";
RL J. Am. Chem. Soc. 128:13036-13037(2006).
RN [4]
RP PATHWAY.
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 conversion of pentalenene to pentalen-13-al by
CC stepwise oxidation via pentalen-13-ol, a precursor of
CC neopentalenolactone antibiotic. {ECO:0000269|PubMed:17017767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + 2 O2 + pentalenene + 4 reduced [2Fe-2S]-[ferredoxin]
CC = 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin] + pentalen-13-al;
CC Xref=Rhea:RHEA:31699, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17251, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:63244; EC=1.14.15.32;
CC Evidence={ECO:0000269|PubMed:17017767};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.62 uM for active enantiomer of pentalenene
CC {ECO:0000269|PubMed:17017767};
CC Note=kcat is 0.503 min(-1) with active enantiomer of pentalenene as
CC substrate.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17017767};
CC -!- PATHWAY: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
CC {ECO:0000269|PubMed:17017767, ECO:0000269|PubMed:21250661}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BA000030; BAC70710.1; -; Genomic_DNA.
DR RefSeq; WP_010984430.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82IY3; -.
DR SMR; Q82IY3; -.
DR STRING; 227882.SAV_2999; -.
DR PRIDE; Q82IY3; -.
DR EnsemblBacteria; BAC70710; BAC70710; SAVERM_2999.
DR KEGG; sma:SAVERM_2999; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_001570_5_1_11; -.
DR OMA; GRSCIGY; -.
DR OrthoDB; 520970at2; -.
DR BioCyc; MetaCyc:MON-16833; -.
DR UniPathway; UPA01021; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:0050467; F:pentalenene synthase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Heme; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..449
FT /note="Pentalenene oxygenase"
FT /id="PRO_0000418751"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 393
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 449 AA; 50757 MW; 20595617E54AD104 CRC64;
MSQHTFVAGT APGAVPVVGH AWQMMRRPLH FMSSLSAHGD LVKIRIGPTS AYVPCHPELL
RQVLTNDRVF DKGGVFYDRA RDIAGNGLVT CPYRDHRRQR RLMQSAFQRT QLERYSTAMR
AEIDATAARW HDGTVIDAFP ELYGMALRTV ARTLYSTPVT EELAQRVEQA FDTVLNGLFR
QMFLPHSLRR LPTPANLRYR NNLRFLHDTV QDLITEYRRD DTQRDDLLSA LLASRDEDGG
RLGDTEIHDQ VITVMAAGTE TVAGTLTWIF HLLSRHPEIE ARLYEEIDTV LDGKPPHWDD
LPSLSLTDRI ITEALRMYPP AWIFTRLTAS DVDLAGVRLP EGTTIVFSPS SVQRHSEAYD
DASRFDPDRW LPDRTSAVAR QAFTAFGTGA RKCIGDLFAR TEATLALATM LSQWRVTVEP
DADVRPVALA TVYHPRRLRL RLTARTPGQ
