P450_LEPMJ
ID P450_LEPMJ Reviewed; 588 AA.
AC E5AE41;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Phomenoic acid biosynthesis cluster cytochrome P450 monooxygenase {ECO:0000303|PubMed:23396262};
DE EC=1.-.-.- {ECO:0000305|PubMed:23396262};
DE Flags: Precursor;
GN Name=P450 {ECO:0000303|PubMed:21326234}; ORFNames=LEMA_P002670;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
RN [2]
RP IDENTIFICATION, FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=23396262; DOI=10.1016/j.fgb.2013.01.008;
RA Elliott C.E., Callahan D.L., Schwenk D., Nett M., Hoffmeister D.,
RA Howlett B.J.;
RT "A gene cluster responsible for biosynthesis of phomenoic acid in the plant
RT pathogenic fungus, Leptosphaeria maculans.";
RL Fungal Genet. Biol. 53:50-58(2013).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of phomenoic acid, a long chain aliphatic
CC carboxylic acid that does not appear to be essential for pathogenicity
CC but may play a role in allowing to outcompete other fungi in the
CC environmental niche via its antifungal properties (PubMed:23396262).
CC The polyketide synthase produces the long methylated aliphatic
CC carboxylic acid chain of phomenoic acid (Probable). The cluster-
CC specific cytochrome P450 monooxygenase may then hydroxylate the methyl
CC group of carbon 31 (Probable). The putative dehydrogenase YogA, which
CC has no obvious role in phomenoic acid biosynthesis, may further modify
CC phomenoic acid to produce a compound not identified yet (Probable).
CC {ECO:0000269|PubMed:23396262, ECO:0000305|PubMed:23396262}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:23396262}.
CC -!- INDUCTION: Expression is positively regulated by the phomenoic acid
CC biosynthesis cluster-specific transcription regulator C6TF.
CC {ECO:0000269|PubMed:23396262}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929139; CBY01480.1; -; Genomic_DNA.
DR RefSeq; XP_003844959.1; XM_003844911.1.
DR AlphaFoldDB; E5AE41; -.
DR SMR; E5AE41; -.
DR STRING; 5022.CBY01480; -.
DR EnsemblFungi; CBY01480; CBY01480; LEMA_P002670.1.
DR GeneID; 13290521; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_25_2_1; -.
DR InParanoid; E5AE41; -.
DR OMA; QEWLFEE; -.
DR OrthoDB; 786853at2759; -.
DR Proteomes; UP000002668; Genome.
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; -; 1.
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 PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..588
FT /note="Phomenoic acid biosynthesis cluster cytochrome P450
FT monooxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000446533"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519
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 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 588 AA; 67246 MW; E335B9F1F820CD27 CRC64;
MSFARIFITI LLLFILRRAF KWLKMIVDAR SIGLPMVFVP MDQTNFLWVL LSSRNRFRLQ
SLLPLWLWKR LSITIPGWEL FEPSNPLETS PTSRTEATDT SFILVGLRTY DFWTADPQVA
HEVLRRIHDF EQPRELEFLL AKFGPNVLTA NGDQWARHRK IVTKVINERI SKAVFESSIY
YCRRILHDVL TTSPDKSSSV ETTMLFDKLT QISFSILIGV GIGDKFPWYD EEKQEPEPPY
QMAYKDALLT YVNNAFGVAI LPPRLLNHWP SWAPGHKKMR TVGRSMTEFC MRNKSLIDQE
QNRIARGETS TSSNADFIAL LVQASQSGED SQQSLSENEM ISNLFAFTAG GYKTIAGALD
FAVVLLARFP LWQDWLIEEV DSLIPADGDG SEPLEYTTIY PQAVRTLAFV METERLYGSA
SRLFRIASGP QTIQVSSGTT VRLPAKTRVH INVVALHHLP SWRDINHQSD PDRFKPSPDA
PDEKLFRPSR WINPPGSKYT HFHPPKGTFV PWSQGPRICP GQKMAQVEIT TLILCLLRRH
RIEPSRLEGE TLQDAERGLD AKLQNVQWGG IVSLEKDPHL KFRVSQRR
