PTAL_PESFW
ID PTAL_PESFW Reviewed; 372 AA.
AC A0A067XMP1; W3WSW3;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Oxidoreductase ptaL {ECO:0000303|PubMed:24302702};
DE EC=1.-.-.- {ECO:0000305|PubMed:24302702};
DE AltName: Full=Pestheic acid biosynthesis cluster protein L {ECO:0000303|PubMed:24302702};
DE Flags: Precursor;
GN Name=ptaL {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10837;
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=24302702; DOI=10.1002/cbic.201300626;
RA Xu X., Liu L., Zhang F., Wang W., Li J., Guo L., Che Y., Liu G.;
RT "Identification of the first diphenyl ether gene cluster for pestheic acid
RT biosynthesis in plant endophyte Pestalotiopsis fici.";
RL ChemBioChem 15:284-292(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- FUNCTION: Oxidoreductase; part of the gene cluster that mediates the
CC biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic
CC precursor of the unique chloropupukeananes (PubMed:24302702). The
CC biosynthesis initiates from condensation of acetate and malonate units
CC catalyzed by the non-reducing PKS ptaA (PubMed:24302702). As the ptaA
CC protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization
CC of the polyketide could be catalyzed by ptaB containing a beta-
CC lactamase domain (PubMed:24302702). The ptaB protein might hydrolyze
CC the thioester bond between the ACP of ptaA and the intermediate to
CC release atrochrysone carboxylic acid, which is spontaneously dehydrated
CC to form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is
CC then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC
CC (PubMed:24302702). Spontaneous decarboxylation of endocrocin occurs to
CC generate emodin (PubMed:24302702). An O-methyltransferase (ptaH or
CC ptaI) could methylate emodin to form physcion (PubMed:24302702). PtaJ
CC could then catalyze the oxidative cleavage of physcion, and rotation of
CC the intermediate could then afford desmethylisosulochrin
CC (PubMed:24302702). PtaF, a putative NADH-dependent oxidoreductase,
CC might also participate in the oxidative cleavage step
CC (PubMed:24302702). Desmethylisosulochrin is then transformed by another
CC O-methyltransferase (ptaH or ptaI) to form isosulochrin
CC (PubMed:24302702). Chlorination of isosulochrin by ptaM in the
CC cyclohexadienone B ring then produces chloroisosulochrin
CC (PubMed:24302702). PtaE is responsible for the oxidative coupling
CC reactions of both benzophenones isosulochrin and chloroisosulochrin to
CC RES-1214-1 and pestheic acid respectively, regardless of chlorination.
CC {ECO:0000269|PubMed:24302702}.
CC -!- COFACTOR:
CC Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470;
CC Evidence={ECO:0000250|UniProtKB:Q9BRQ8};
CC Note=Binds 6-hydroxy-FAD non-covalently.
CC {ECO:0000250|UniProtKB:Q9BRQ8};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:24302702}.
CC -!- INDUCTION: The cluster is expressed in rice fermentation medium
CC (PubMed:25623211). Three regulators are located in the cluster (ptaR1,
CC ptaR2 and ptaR3), suggesting that the production of pestheic acid is
CC controlled by a complex regulatory mechanism (PubMed:24302702).
CC {ECO:0000269|PubMed:25623211, ECO:0000305|PubMed:24302702}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ETS76963.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KC145148; AGO59047.1; -; Genomic_DNA.
DR EMBL; KI912116; ETS76963.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_007837609.1; XM_007839418.1.
DR AlphaFoldDB; A0A067XMP1; -.
DR SMR; A0A067XMP1; -.
DR STRING; 393283.XP_007837609.1; -.
DR EnsemblFungi; ETS76963; ETS76963; PFICI_10837.
DR GeneID; 19275850; -.
DR KEGG; pfy:PFICI_10837; -.
DR eggNOG; KOG2495; Eukaryota.
DR OrthoDB; 1463391at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..372
FT /note="Oxidoreductase ptaL"
FT /id="PRO_0000443051"
FT BINDING 8..12
FT /ligand="6-hydroxy-FAD"
FT /ligand_id="ChEBI:CHEBI:60470"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="6-hydroxy-FAD"
FT /ligand_id="ChEBI:CHEBI:60470"
FT /evidence="ECO:0000255"
FT BINDING 285
FT /ligand="6-hydroxy-FAD"
FT /ligand_id="ChEBI:CHEBI:60470"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 372 AA; 39845 MW; 93C7369F2BADB9FB CRC64;
MKHIVIIGGG FAGVSTAHRF LKNVGKSTTA PYKVTLVSRD SHFFWNIAAP RGIIPGQIPE
EKLFQPIAEG FSQYGPDKFE FVLGTATDLD VGGKTLVVDV DGKATRISYD YLIIGSGSRT
KIPGPFKSDG STDGVKQTIH DFQERVKAAK TIVVVGAGPT GVETAGELAF EYGTSKKIIL
ISGGPTVLEN RPASVTKTAL KQLETLNVDV RVNTKAKDPV TLPDGKKELT LSGGEKLVVD
LYIPTFGVLP NSSFVPSQYL DSNGFVQVDQ YFQVKGAEGV FAIGDVSDSE APQFWFVEKQ
SVHIAKNLIL SLSGKAPTPY KASATGMMGL QIGKNSGTGH FGNFKLPGFL VKTIRKTLFV
ENLPKTVDGS ML
