PK81D_PSEFD
ID PK81D_PSEFD Reviewed; 492 AA.
AC M3A333;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Cytochrome P450 monooxygenase MYCFIDRAFT_204672 {ECO:0000303|PubMed:30735556};
DE EC=1.14.13.- {ECO:0000305|PubMed:30735556};
DE AltName: Full=PKS8-1 gene cluster protein MYCFIDRAFT_204672 {ECO:0000303|PubMed:30735556};
GN ORFNames=MYCFIDRAFT_204672;
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=27388157; DOI=10.1371/journal.pone.0158471;
RA Noar R.D., Daub M.E.;
RT "Bioinformatics prediction of polyketide synthase gene clusters from
RT Mycosphaerella fijiensis.";
RL PLoS ONE 11:e0158471-e0158471(2016).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30735556; DOI=10.1371/journal.pone.0212229;
RA Noar R.D., Thomas E., Daub M.E.;
RT "A novel polyketide synthase gene cluster in the plant pathogenic fungus
RT Pseudocercospora fijiensis.";
RL PLoS ONE 14:e0212229-e0212229(2019).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of an emodin derivative that may be involved
CC in black Sigatoka disease of banana (PubMed:27388157, PubMed:30735556).
CC The pathway begins with the synthesis of atrochrysone thioester by the
CC polyketide synthase PKS8-1 (Probable). The atrochrysone carboxyl ACP
CC thioesterase MYCFIDRAFT_190111 then breaks the thioester bond and
CC releases the atrochrysone carboxylic acid from PKS8-1 (Probable). The
CC decarboxylase MYCFIDRAFT_34057 then catalyzes the concerted
CC decarboxylation-elimination required to convert atochrysone carboxylic
CC acid into emodin anthrone, which is further oxidized to emodin by the
CC anthrone oxygenase MYCFIDRAFT_34418 (Probable). The functions of the
CC other tailoring enzymes as well as the final product of the cluster
CC have still to be identified (Probable). {ECO:0000269|PubMed:27388157,
CC ECO:0000269|PubMed:30735556, ECO:0000305|PubMed:30735556}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30735556}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor MYCFIDRAFT_198930 and is up-regulated during
CC banana leaves infection. {ECO:0000269|PubMed:30735556}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KB446562; EME79061.1; -; Genomic_DNA.
DR RefSeq; XP_007929885.1; XM_007931694.1.
DR AlphaFoldDB; M3A333; -.
DR SMR; M3A333; -.
DR EnsemblFungi; EME79061; EME79061; MYCFIDRAFT_204672.
DR GeneID; 19336302; -.
DR KEGG; pfj:MYCFIDRAFT_204672; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_033574_2_0_1; -.
DR OrthoDB; 825914at2759; -.
DR Proteomes; UP000016932; 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; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Cytochrome P450 monooxygenase MYCFIDRAFT_204672"
FT /id="PRO_0000451121"
FT TRANSMEM 269..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 430
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 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 492 AA; 55499 MW; 81587B0D8D0FB42C CRC64;
MALGFLVYLS YTPRIKGNIP AFTPETYPII GSYKFFTHKL SFWKAAQRAS KNGMFSFWLG
KNHVVGVSGE AARKMYLENP AMDHIKGVIL IGHGPDYIDG RKTKQHGIWL PVMAGNKSYA
QKNVLNCQKT AELTKRLPKV TNDVRKAFES VASQGFIINP ARMCAVLTWD TATRVFAADE
LIDVPENRAK LLYYLPILQK TSSCHLLSFP WASYFSLPYW KRKYGREGMR RLVTPIVEAR
MRIIDPVRAD DPLQTFVDNG DSADYMINFL ISMIFISAAN GCVVSGAMLY SIAHHPELQE
KIYQEIKAAA NQYAADSSAP LVDQLDSLPV KAWENMSETI DLCYKECIRM WVAFPMGRMN
EGTTDIKIPG TDEVVPAGGL CCYNTIDVHY SEKLYPEPLK WDPARFGEGR KEMEQEAHGF
MGWGAGRHPC NGIRWAKIQQ NMMLAYAFAM YKWTGCHKDG SPNTDFIPPT TALNELAPSL
PQNLFLKAEP RK
