PPZD_METRR
ID PPZD_METRR Reviewed; 353 AA.
AC A0A166YZY4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=2-oxoglutarate-Fe(II) type oxidoreductase ppzD {ECO:0000303|PubMed:30452111};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=Pyrrolopyrazine biosynthesis cluster protein D {ECO:0000303|PubMed:30452111};
GN Name=ppzD {ECO:0000303|PubMed:30452111}; ORFNames=NOR_07096;
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: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene
CC cluster that mediates the biosynthesis of pyrrolopyrazines, secondary
CC metabolites 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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30452111}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AZHC01000030; OAA37397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166YZY4; -.
DR SMR; A0A166YZY4; -.
DR EnsemblFungi; OAA37397; OAA37397; NOR_07096.
DR OrthoDB; 622449at2759; -.
DR Proteomes; UP000243498; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..353
FT /note="2-oxoglutarate-Fe(II) type oxidoreductase ppzD"
FT /id="PRO_0000450258"
FT DOMAIN 181..292
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 283
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 353 AA; 39996 MW; 347AB886696229A9 CRC64;
MARTPERRVR TLDFAQFCHG EPSSSHGFCR ELVDCLRSLG FVKIRNHGIS GEEIEKVFVM
NKLFFSLPQA AKAKAAHPPE ANPHRGYSYV GQEKLSRVKD YEKGKRSIVD VYDIKESYDQ
GPAVDKLYPN RWPDKQDIPG FRVVMEKFYE RCHQVHQDVL RAIATGFDLS PSFLTDLCCE
NTSELRLNHY PGVHPSSLRK GAKRISEHTD FGTVTLLFQD SVGGLEIEDQ NSPGTYFPVS
SERKSDMIVN VGDCIQRWTN DKILSTSHRV VLPEDRDALI KDRYSVAYFG KPSRSQLVSP
LREFVKEGEK PKYSAISAWQ YNQEKLVLTY GGDEEILVPK PSSSVCTGVG QLQ
