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Oxidoreductase ptaL (EC 1.-.-.-) (Pestheic acid biosynthesis cluster protein L)

 PTAL_PESFW              Reviewed;         372 AA.
A0A067XMP1; W3WSW3;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
01-OCT-2014, sequence version 1.
23-MAY-2018, entry version 16.
RecName: Full=Oxidoreductase ptaL {ECO:0000303|PubMed:24302702};
EC=1.-.-.- {ECO:0000305|PubMed:24302702};
AltName: Full=Pestheic acid biosynthesis cluster protein L {ECO:0000303|PubMed:24302702};
Flags: Precursor;
Name=ptaL {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10837;
Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
Pestalotiopsis.
NCBI_TaxID=1229662;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
STRAIN=W106-1 / CGMCC3.15140;
PubMed=24302702; DOI=10.1002/cbic.201300626;
Xu X., Liu L., Zhang F., Wang W., Li J., Guo L., Che Y., Liu G.;
"Identification of the first diphenyl ether gene cluster for pestheic
acid biosynthesis in plant endophyte Pestalotiopsis fici.";
ChemBioChem 15:284-292(2014).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
STRAIN=W106-1 / CGMCC3.15140;
PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
"Genomic and transcriptomic analysis of the endophytic fungus
Pestalotiopsis fici reveals its lifestyle and high potential for
synthesis of natural products.";
BMC Genomics 16:28-28(2015).
-!- FUNCTION: Oxidoreductase; part of the gene cluster that mediates
the biosynthesis of pestheic acid, a diphenyl ether which is a
biosynthetic precursor of the unique chloropupukeananes
(PubMed:24302702). The biosynthesis initiates from condensation of
acetate and malonate units catalyzed by the non-reducing PKS ptaA
(PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient,
hydrolysis and Claisen cyclization of the polyketide could be
catalyzed by ptaB containing a beta-lactamase domain
(PubMed:24302702). The ptaB protein might hydrolyze the thioester
bond between the ACP of ptaA and the intermediate to release
atrochrysone carboxylic acid, which is spontaneously dehydrated to
form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is
then converted to endocrocin, catalyzed by the anthrone oxygenase
ptaC (PubMed:24302702). Spontaneous decarboxylation of endocrocin
occurs to generate emodin (PubMed:24302702). An O-
methyltransferase (ptaH or ptaI) could methylate emodin to form
physcion (PubMed:24302702). PtaJ could then catalyze the oxidative
cleavage of physcion, and rotation of the intermediate could then
afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative
NADH-dependent oxidoreductase, might also participate in the
oxidative cleavage step (PubMed:24302702). Desmethylisosulochrin
is then transformed by another O-methyltransferase (ptaH or ptaJ)
to form isosulochrin (PubMed:24302702). Chlorination of
isosulochrin by ptaM in the cyclohexadienone B ring then produces
chloroisosulochrin (PubMed:24302702). PtaE is responsible for the
oxidative coupling reactions of both benzophenones isosulochrin
and chloroisosulochrin to RES-1214-1 and pestheic acid
respectively, regardless of chlorination.
{ECO:0000269|PubMed:24302702}.
-!- COFACTOR:
Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470;
Evidence={ECO:0000250|UniProtKB:Q9BRQ8};
Note=Binds 6-hydroxy-FAD non-covalently.
{ECO:0000250|UniProtKB:Q9BRQ8};
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000305|PubMed:24302702}.
-!- INDUCTION: The cluster is expressed in rice fermentation medium
(PubMed:25623211). Three regulators are located in the cluster
(ptaR1, ptaR2 and ptaR3), suggesting that the production of
pestheic acid is controlled by a complex regulatory mechanism
(PubMed:24302702). {ECO:0000269|PubMed:25623211,
ECO:0000305|PubMed:24302702}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ETS76963.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; KC145148; AGO59047.1; -; Genomic_DNA.
EMBL; KI912116; ETS76963.1; ALT_INIT; Genomic_DNA.
RefSeq; XP_007837609.1; XM_007839418.1.
ProteinModelPortal; A0A067XMP1; -.
SMR; A0A067XMP1; -.
EnsemblFungi; ETS76963; ETS76963; PFICI_10837.
GeneID; 19275850; -.
KEGG; pfy:PFICI_10837; -.
Proteomes; UP000030651; Unassembled WGS sequence.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Pfam; PF07992; Pyr_redox_2; 1.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51905; SSF51905; 1.
2: Evidence at transcript level;
Complete proteome; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
Reference proteome; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 372 Oxidoreductase ptaL.
/FTId=PRO_0000443051.
NP_BIND 8 12 6-hydroxy-FAD. {ECO:0000255}.
BINDING 51 51 6-hydroxy-FAD. {ECO:0000255}.
BINDING 285 285 6-hydroxy-FAD. {ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
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


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