ID   PATJ_ASPCL              Reviewed;         323 AA.
AC   A1CFL7;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable oxidoreductase patJ {ECO:0000250|UniProtKB:J5J930};
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:J5J930};
DE   AltName: Full=Patulin synthesis protein J {ECO:0000303|PubMed:19383676};
GN   Name=patJ {ECO:0000303|PubMed:19383676}; ORFNames=ACLA_093650;
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: Probable oxidoreductase; part of the gene cluster that
CC       mediates the biosynthesis of patulin, an acetate-derived tetraketide
CC       mycotoxin produced by several fungal species that shows antimicrobial
CC       properties against several bacteria (By similarity). PatJ acts with
CC       patO in the vacuole to convert gentisyl alcohol to isoepoxydon (By
CC       similarity). The pathway begins with the synthesis of 6-methylsalicylic
CC       acid by the polyketide synthase (PKS) patK via condensation of acetate
CC       and malonate units. The 6-methylsalicylic acid decarboxylase patG then
CC       catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-
CC       cresol (also known as 3-methylphenol). These first reactions occur in
CC       the cytosol. The intermediate m-cresol is then transported into the
CC       endoplasmic reticulum where the cytochrome P450 monooxygenase patH
CC       converts it to m-hydroxybenzyl alcohol, which is further converted to
CC       gentisyl alcohol by the cytochrome P450 monooxygenase patI. The
CC       oxidoreductases patJ and patO further convert gentisyl alcohol to
CC       isoepoxydon in the vacuole. PatN catalyzes then the transformation of
CC       isoepoxydon into phyllostine. The cluster protein patF is responsible
CC       for the conversion from phyllostine to neopatulin whereas the alcohol
CC       dehydrogenase patD converts neopatulin to E-ascladiol. The steps
CC       between isoepoxydon and E-ascladiol occur in the cytosol, and E-
CC       ascladiol is probably secreted to the extracellular space by one of the
CC       cluster-specific transporters patC or patM. Finally, the secreted
CC       patulin synthase patE catalyzes the conversion of E-ascladiol to
CC       patulin (PubMed:19383676) (Probable).
CC       {ECO:0000250|UniProtKB:A0A075TR41, ECO:0000305|PubMed:19383676}.
CC   -!- PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis.
CC       {ECO:0000305|PubMed:19383676}.
CC   -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000250|UniProtKB:A0A075TR41}.
CC       Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:A0A075TR41}.
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 oxidoreductase OpS7 family. {ECO:0000305}.
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DR   EMBL; DS027052; EAW11666.1; -; Genomic_DNA.
DR   RefSeq; XP_001273092.1; XM_001273091.1.
DR   AlphaFoldDB; A1CFL7; -.
DR   SMR; A1CFL7; -.
DR   PRIDE; A1CFL7; -.
DR   EnsemblFungi; EAW11666; EAW11666; ACLA_093650.
DR   GeneID; 4704854; -.
DR   KEGG; act:ACLA_093650; -.
DR   VEuPathDB; FungiDB:ACLA_093650; -.
DR   eggNOG; ENOG502R8E2; Eukaryota.
DR   HOGENOM; CLU_068080_0_0_1; -.
DR   OMA; GYKPFFR; -.
DR   OrthoDB; 1423082at2759; -.
DR   UniPathway; UPA00918; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; ISS:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0140723; P:patulin biosynthetic process; ISS:GO_Central.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Oxidoreductase; Reference proteome; Vacuole.
FT   CHAIN           1..323
FT                   /note="Probable oxidoreductase patJ"
FT                   /id="PRO_0000437118"
FT   REGION          291..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  36668 MW;  B4DE103CA8BCC2F6 CRC64;
     MAPFVPYHSS AGQATIVKFG GLLTTEFLEP PPGRCFLFRQ TYRHTVEGPI PENLRKLINS
     PHKPKGPPPH FHQFQTEYFR VETGVLGIEV DGVLRRITPE DGEISVKAGS VHRFFIHPDS
     PESMTVYLSA SDSGNDYQLD RIFFENWYGY WHDALLHDGG IDWIQFLAIQ DGGDAYTPAP
     AWVPFRRQVG YWTCVIVGRW IGGLLGYKPF FREYTTDWDF AVAKMKGSVF QRHLVHEAFG
     AEKSWKQQTE LEARVKPENA EFEQWTEDMS PTPLMLKPLA YEAGEFKGLQ DQSANGVNGH
     ATGVEAKKKQ LGDMTRRRSG AQE