PPZE_METRR
ID PPZE_METRR Reviewed; 392 AA.
AC A0A166YZU9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Cytochrome P450 monooxygenase ppzE {ECO:0000303|PubMed:30452111};
DE EC=1.-.-.- {ECO:0000305|PubMed:30452111};
DE AltName: Full=Pyrrolopyrazine biosynthesis cluster protein E {ECO:0000303|PubMed:30452111};
GN Name=ppzE {ECO:0000303|PubMed:30452111}; ORFNames=NOR_07094;
OS Metarhizium rileyi (strain RCEF 4871) (Nomuraea rileyi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 4871;
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=30452111; DOI=10.1111/1462-2920.14483;
RA Berry D., Mace W., Rehner S.A., Grage K., Dijkwel P.P., Young C.A.,
RA Scott B.;
RT "Orthologous peramine and pyrrolopyrazine-producing biosynthetic gene
RT clusters in Metarhizium rileyi, Metarhizium majus and Cladonia grayi.";
RL Environ. Microbiol. 21:928-939(2019).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of pyrrolopyrazines, secondary metabolites
CC showing insecticidal activity (PubMed:30452111). The single
CC multifunctional NRPS ppzA is responsible for the biosynthesis of
CC peramine (PubMed:30452111). The condensation domain of ppzA is proposed
CC to catalyze formation of a peptide bond between 1-pyrroline-5-
CC carboxylate and arginine (By similarity). The methylation domain of
CC ppzA would catalyze the N-methylation of the alpha-amino group of
CC arginine (By similarity). The reductase domain is proposed to be
CC responsible for reduction of the thioester and the cyclization to form
CC an iminium ion resulting in release from the peptide synthetase (By
CC similarity). Deprotonation of this intermediate and oxidation of the
CC pyrroline ring would give rise to peramine (By similarity). This final
CC oxidation to give the pyrrole functionality may be spontaneous (By
CC similarity). In Epichloe species that produce only peramine, the
CC peramine synthetase gene is not localized in a gene cluster, in
CC contrast to Metarhizium rileyi that contains additionnal
CC pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-
CC Fe(II) type oxidoreductases ppzC and ppzD could be candidates for
CC conversion of proline into an oxidized derivative to be used by the
CC ppzA A1-domain as substrate (Probable). The other ppz genes encode
CC proteins predicted to derivatize peramine into more complex
CC pyrrolopyrazine metabolites (Probable). {ECO:0000250|UniProtKB:Q4H424,
CC ECO:0000269|PubMed:30452111, ECO:0000305|PubMed:30452111}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30452111}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AZHC01000030; OAA37395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166YZU9; -.
DR SMR; A0A166YZU9; -.
DR STRING; 1081105.A0A166YZU9; -.
DR EnsemblFungi; OAA37395; OAA37395; NOR_07094.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000243498; Unassembled WGS sequence.
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 Gene3D; 1.10.630.10; -; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..392
FT /note="Cytochrome P450 monooxygenase ppzE"
FT /id="PRO_0000450263"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 353
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|UniProtKB:P04798"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 392 AA; 44641 MW; 7AAF7E1ECA7CDBC5 CRC64;
MLSIIHVGWL ELVWFVALYP FACWTLFAVL KSVYRITLHP LAKFPGPKLA GASYCYEFWY
EIVCGIQYTQ KIIKLHEQYG PIVRINPDEL HFNDIDFVDV VYTAGARKRD KSRHYLAGFE
GSIIRFVSSD FHSFLIDTRV KKPERLKRVV LGAERHHDAK DCPMFLELLN SNLPAQEKSK
QRLMYEANGA TLAGSGSTAI ALSNIVYNLV ANPRIGHKLR SELMRKVSAS KNLPTWSTLE
ELPYLTAVIH EGLRSMYDPS KERLPYDPSQ ERLPRVATEE ELIYEGGSAL GKSKYVIPRG
YAISTSAHVV HSDESIFPNA SQFDPERWLD RDGQRNKELE RHLLSFSKGS RHCLGMHCRR
ATCLAIPASA RNGTSGYQFT SGQLEYKVQE RQ
