PATB_PENEN
ID PATB_PENEN Reviewed; 561 AA.
AC A0A075TXZ3;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Carboxylesterase patB {ECO:0000303|PubMed:25120234};
DE EC=3.1.1.1 {ECO:0000305|PubMed:25120234};
DE AltName: Full=Patulin biosynthesis cluster protein B {ECO:0000303|PubMed:25120234};
DE Flags: Precursor;
GN Name=patB {ECO:0000303|PubMed:25120234}; ORFNames=PEX2_082800;
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, INDUCTION, AND
RP PATHWAY.
RC STRAIN=NRRL 35695;
RX PubMed=25120234; DOI=10.1016/j.ijfoodmicro.2014.07.028;
RA Tannous J., El Khoury R., Snini S.P., Lippi Y., El Khoury A., Atoui A.,
RA Lteif R., Oswald I.P., Puel O.;
RT "Sequencing, physical organization and kinetic expression of the patulin
RT biosynthetic gene cluster from Penicillium expansum.";
RL Int. J. Food Microbiol. 189C:51-60(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8;
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
RN [3]
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 [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).
RN [6]
RP INDUCTION.
RX PubMed=27528575; DOI=10.1111/mpp.12469;
RA Kumar D., Barad S., Chen Y., Luo X., Tannous J., Dubey A., Glam Matana N.,
RA Tian S., Li B., Keller N., Prusky D.;
RT "LaeA regulation of secondary metabolism modulates virulence in Penicillium
RT expansum and is mediated by sucrose.";
RL Mol. Plant Pathol. 18:1150-1163(2017).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=30100914; DOI=10.3389/fpls.2018.01094;
RA Kumar D., Tannous J., Sionov E., Keller N., Prusky D.;
RT "Apple intrinsic factors modulating the global regulator, LaeA, the patulin
RT gene cluster and patulin accumulation during fruit colonization by
RT Penicillium expansum.";
RL Front. Plant Sci. 9:1094-1094(2018).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=25625822; DOI=10.1094/mpmi-12-14-0398-fi;
RA Li B., Zong Y., Du Z., Chen Y., Zhang Z., Qin G., Zhao W., Tian S.;
RT "Genomic characterization reveals insights into patulin biosynthesis and
RT pathogenicity in Penicillium species.";
RL Mol. Plant Microbe Interact. 28:635-647(2015).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION, AND
RP PATHWAY.
RX PubMed=30680886; DOI=10.1111/1462-2920.14542;
RA Li B., Chen Y., Zong Y., Shang Y., Zhang Z., Xu X., Wang X., Long M.,
RA Tian S.;
RT "Dissection of patulin biosynthesis, spatial control and regulation
RT mechanism in Penicillium expansum.";
RL Environ. Microbiol. 21:1124-1139(2019).
CC -!- FUNCTION: Carboxylesterase; part of the gene cluster that mediates the
CC biosynthesis of patulin, an acetate-derived tetraketide mycotoxin
CC produced by several fungal species that shows antimicrobial properties
CC against several bacteria (PubMed:30100914, PubMed:25625822,
CC PubMed:30680886). The function of patB in patulin synthesis has still
CC to be characterized (PubMed:30680886). The pathway begins with the
CC synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS)
CC patK via condensation of acetate and malonate units. The 6-
CC methylsalicylic acid decarboxylase patG then catalyzes the
CC decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known
CC as 3-methylphenol). These first reactions occur in the cytosol. The
CC intermediate m-cresol is then transported into the endoplasmic
CC reticulum where the cytochrome P450 monooxygenase patH converts it to
CC m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol
CC by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and
CC patO further convert gentisyl alcohol to isoepoxydon in the vacuole.
CC PatN catalyzes then the transformation of isoepoxydon into phyllostine.
CC The cluster protein patF is responsible for the conversion from
CC phyllostine to neopatulin whereas the alcohol dehydrogenase patD
CC converts neopatulin to E-ascladiol. The steps between isoepoxydon and
CC E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted
CC to the extracellular space by one of the cluster-specific transporters
CC patC or patM. Finally, the secreted patulin synthase patE catalyzes the
CC conversion of E-ascladiol to patulin (PubMed:30680886) (Probable).
CC {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914,
CC ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC -!- PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis.
CC {ECO:0000269|PubMed:30680886}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
CC -!- INDUCTION: Expression is correlated with the production of patulin
CC (PubMed:25120234). Expression is positively regulated by the secondary
CC metabolism regulator laeA (PubMed:27528575, PubMed:30100914).
CC Expression is strongly decreased with increased sucrose concentrations.
CC This decrease is lost in the presence of malic acid (PubMed:30100914).
CC Expression is increased with pH changes from 2.5 to 3.5 in the presence
CC of a limiting concentration of sucrose, 50 mM (PubMed:30100914).
CC Natural phenols present in apple fruits such as chlorogenic acid or the
CC flavonoid epicatechin modulate patulin biosynthesis. They increase
CC expression in the absence of sucrose, have little impact in the
CC presence of 15 mM sucrose, and decrease expression in 175 mM sucrose
CC (PubMed:30100914). Expression is positively regulated by the patulin
CC cluster-specific transcription factor patL (PubMed:25625822). Finally,
CC expression is also positively regulated by the velvet family proteins
CC transcription regulators veA, velB, velC, but not vosA
CC (PubMed:30680886). {ECO:0000269|PubMed:25120234,
CC ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:27528575,
CC ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduces the production of patulin.
CC {ECO:0000269|PubMed:30680886}.
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 type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; KF899892; AIG62138.1; -; Genomic_DNA.
DR EMBL; JQFZ01000262; KGO52633.1; -; Genomic_DNA.
DR RefSeq; XP_016595363.1; XM_016745550.1.
DR AlphaFoldDB; A0A075TXZ3; -.
DR SMR; A0A075TXZ3; -.
DR STRING; 27334.A0A075TXZ3; -.
DR ESTHER; penen-a0a075txz3; Fungal_carboxylesterase_lipase.
DR EnsemblFungi; KGO43537; KGO43537; PEXP_094380.
DR EnsemblFungi; KGO52633; KGO52633; PEX2_082800.
DR EnsemblFungi; KGO61366; KGO61366; PEX1_005130.
DR GeneID; 27680970; -.
DR HOGENOM; CLU_006586_10_5_1; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; A0A075TXZ3; -.
DR UniPathway; UPA00918; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..561
FT /note="Carboxylesterase patB"
FT /evidence="ECO:0000255"
FT /id="PRO_5007947098"
FT ACT_SITE 263
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 385
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P22303"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22303"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 561 AA; 61487 MW; FB6F1F4CF32329E3 CRC64;
MQIINWASLL LVTWETVVAA ELPIVDLGYQ RHQAIGFNST GRYYQFSNVR YAEPPLGPLR
FSLPVSPRNR SHEVVNGKGL GNICPQSQAC WFNVQGDFVS AVTAGSTFNF TAAYDQVYQQ
DECTKPRPVA DQNPLESEDC LFLDVYVPEK VISKRRDGNG KSNPGAPVLV YFQDGAYVSG
SKSDQNPSGL IATSREDGST GIIYVGVNYR LGVFGWLSGQ KFQSEGGLPN AGLYDERLAL
EWVQRHITKF GGDPSRVTVM GVSAGGGSIT MQLTAYGRAI RPPFAQIIAQ SPAWEPGTKT
PAIEDDLLDS FLTLLNVSSL EEARRLPSQA LLDANYELVA SRPYGSGVFG PAIDGSFVPD
SPKRLLLERK VDPSVRILTS YTANEGFMLA PANVTDDATF NRYVDVLLRG ANASVRAHTS
RVLYPPIFNG SWPYHSQHER ANLLWSEVST TCNTRYLHQA VATPGYAIEY AVKPAMHLSD
TSSVFYNGQG SSSSLNATIA QLMQRQIVQF VKTGNPNVKG DPHVPLYHGQ AHVLSLGDNG
VRVEPALTNT DRCTYWQQVE F
