PATF_ASPCL
ID PATF_ASPCL Reviewed; 198 AA.
AC A1CFL3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Patulin synthesis protein F {ECO:0000303|PubMed:19383676};
DE EC=1.-.-.- {ECO:0000250|UniProtKB:A0A075TR27};
DE Flags: Precursor;
GN Name=patF {ECO:0000303|PubMed:19383676}; ORFNames=ACLA_093610;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=15082620; DOI=10.1093/ije/dyh028;
RG Patulin Clinical Trials Committee, Medical Research Council;
RT "Clinical trial of patulin in the common cold. 1944.";
RL Int. J. Epidemiol. 33:243-246(2004).
RN [3]
RP FUNCTION.
RX PubMed=19383676; DOI=10.1099/mic.0.024836-0;
RA Artigot M.P., Loiseau N., Laffitte J., Mas-Reguieg L., Tadrist S.,
RA Oswald I.P., Puel O.;
RT "Molecular cloning and functional characterization of two CYP619 cytochrome
RT P450s involved in biosynthesis of patulin in Aspergillus clavatus.";
RL Microbiology 155:1738-1747(2009).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=22222931; DOI=10.1016/j.fct.2011.12.022;
RA de Melo F.T., de Oliveira I.M., Greggio S., Dacosta J.C., Guecheva T.N.,
RA Saffi J., Henriques J.A., Rosa R.M.;
RT "DNA damage in organs of mice treated acutely with patulin, a known
RT mycotoxin.";
RL Food Chem. Toxicol. 50:3548-3555(2012).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=26619846; DOI=10.1007/s13277-015-4474-z;
RA Boussabbeh M., Ben Salem I., Rjiba-Touati K., Bouyahya C., Neffati F.,
RA Najjar M.F., Bacha H., Abid-Essefi S.;
RT "The potential effect of patulin on mice bearing melanoma cells: an anti-
RT tumour or carcinogenic effect?";
RL Tumor Biol. 37:6285-6295(2016).
CC -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC patulin, an acetate-derived tetraketide mycotoxin produced by several
CC fungal species that shows antimicrobial properties against several
CC bacteria (By similarity). PatF catalyzes the conversion of phyllostine
CC into neopatulin (By similarity). The pathway begins with the synthesis
CC of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via
CC condensation of acetate and malonate units. The 6-methylsalicylic acid
CC decarboxylase patG then catalyzes the decarboxylation of 6-
CC methylsalicylic acid to yield m-cresol (also known as 3-methylphenol).
CC These first reactions occur in the cytosol. The intermediate m-cresol
CC is then transported into the endoplasmic reticulum where the cytochrome
CC P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which
CC is further converted to gentisyl alcohol by the cytochrome P450
CC monooxygenase patI. The oxidoreductases patJ and patO further convert
CC gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the
CC transformation of isoepoxydon into phyllostine. The cluster protein
CC patF is responsible for the conversion from phyllostine to neopatulin
CC whereas the alcohol dehydrogenase patD converts neopatulin to E-
CC ascladiol. The steps between isoepoxydon and E-ascladiol occur in the
CC cytosol, and E-ascladiol is probably secreted to the extracellular
CC space by one of the cluster-specific transporters patC or patM.
CC Finally, the secreted patulin synthase patE catalyzes the conversion of
CC E-ascladiol to patulin (PubMed:19383676) (Probable).
CC {ECO:0000250|UniProtKB:A0A075TR27, ECO:0000305|PubMed:19383676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phyllostine = neopatulin; Xref=Rhea:RHEA:62220,
CC ChEBI:CHEBI:145110, ChEBI:CHEBI:145111;
CC Evidence={ECO:0000250|UniProtKB:A0A075TR27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62221;
CC Evidence={ECO:0000250|UniProtKB:A0A075TR27};
CC -!- PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis.
CC {ECO:0000305|PubMed:19383676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A0A075TR27}.
CC -!- BIOTECHNOLOGY: Patulin was originally used as an antibiotic and
CC specifically trialed to be used against the common cold, but it is no
CC longer used for that purpose since it has been shown to induce
CC immunological, neurological and gastrointestinal effects
CC (PubMed:15082620). Genotoxic effects of patulin with dose-dependent
CC increase in DNA strand breaks in brain, liver and kidneys have been
CC detected in mice (PubMed:22222931). However, more recently, it has been
CC proposed that patulin might also have anti-tumor properties
CC (PubMed:26619846). {ECO:0000269|PubMed:15082620,
CC ECO:0000269|PubMed:22222931, ECO:0000269|PubMed:26619846}.
CC -!- SIMILARITY: Belongs to the patF family. {ECO:0000305}.
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DR EMBL; DS027052; EAW11662.1; -; Genomic_DNA.
DR RefSeq; XP_001273088.1; XM_001273087.1.
DR AlphaFoldDB; A1CFL3; -.
DR SMR; A1CFL3; -.
DR EnsemblFungi; EAW11662; EAW11662; ACLA_093610.
DR GeneID; 4704850; -.
DR KEGG; act:ACLA_093610; -.
DR VEuPathDB; FungiDB:ACLA_093610; -.
DR eggNOG; ENOG502RPD2; Eukaryota.
DR HOGENOM; CLU_119119_0_0_1; -.
DR OMA; FTIDYIF; -.
DR OrthoDB; 1400674at2759; -.
DR UniPathway; UPA00918; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:GO_Central.
DR GO; GO:0140723; P:patulin biosynthetic process; ISS:GO_Central.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..198
FT /note="Patulin synthesis protein F"
FT /evidence="ECO:0000255"
FT /id="PRO_5002633070"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 198 AA; 21825 MW; 85742771178A78F4 CRC64;
MRLSTVLLGS LLGALTQAAP TGQFPGHYQS SPPPLGPSNW ERNPVSVFFK VLNTQPDPDY
TMLKELVTYD CTYVSLTFDN PTLHSIMPWA GTHTNIGPQA FIDIFTRVGL YWDRGPFTID
YIFGDGGNVT AWGSFTATSR TLGKTVISPW AARARVNEDN RIFYFQWMED TFTTASSFGS
DASNKTYVSN PQGGTTVA
