PATB_ASPCL
ID PATB_ASPCL Reviewed; 555 AA.
AC A1CFK9;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Carboxylesterase patB {ECO:0000303|PubMed:19383676};
DE EC=3.1.1.1 {ECO:0000305|PubMed:19383676};
DE AltName: Full=Patulin synthesis protein B {ECO:0000303|PubMed:19383676};
DE Flags: Precursor;
GN Name=patB {ECO:0000303|PubMed:19383676}; ORFNames=ACLA_093570;
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: 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 (By similarity). The function of patB in
CC patulin synthesis has still to be characterized (By similarity). The
CC pathway begins with the synthesis of 6-methylsalicylic acid by the
CC polyketide synthase (PKS) patK via condensation of acetate and malonate
CC units. The 6-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:19383676) (Probable).
CC {ECO:0000250|UniProtKB:A0A075TXZ3, ECO:0000305|PubMed:19383676}.
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:0000305|PubMed:19383676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A0A075TXZ3}.
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; DS027052; EAW11658.1; -; Genomic_DNA.
DR RefSeq; XP_001273084.1; XM_001273083.1.
DR AlphaFoldDB; A1CFK9; -.
DR SMR; A1CFK9; -.
DR STRING; 344612.A1CFK9; -.
DR ESTHER; aspcl-a1cfk9; Fungal_carboxylesterase_lipase.
DR EnsemblFungi; EAW11658; EAW11658; ACLA_093570.
DR GeneID; 4704864; -.
DR KEGG; act:ACLA_093570; -.
DR VEuPathDB; FungiDB:ACLA_093570; -.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_006586_10_5_1; -.
DR OMA; SCNTRYL; -.
DR OrthoDB; 754103at2759; -.
DR UniPathway; UPA00918; -.
DR Proteomes; UP000006701; 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..555
FT /note="Carboxylesterase patB"
FT /id="PRO_5005120964"
FT ACT_SITE 258
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P22303"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22303"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 555 AA; 59936 MW; 41EFFD5288E22251 CRC64;
MLFTASLLLL LPWASAAPAN LPIVDLGYQR HQAISFNSTG QYYSFTNIRY AEPPLGSRRF
APPVAPHGRS KNIVNGTGLG YKCPQALACW FNVQNKFTSA AAAGTPFDFN AAYEEVYTKD
ACTEPAKQDP LQSEDCLFLD VYVPQDVWQK GPQAAHQKGG APVLVYLQDG AYVGGSKSDQ
NPAGLIARSR EEGSSGMIYV GINYRLGVFG WLSGRKFTSS GGKPNAGLLD QRLALEWIQR
HIHLFGGDPS RVTVMGVSAG GGSIIMQMTA YGRGISPPFA QVITQSPAWE PGTKTPAIED
DLFDTFLASL NVTSLDQARR LPSHALTDAN YRLVASRPYG AGVLGPAIDG DFIPDSPKRL
LLQGKANPGV RVLTSYTAAE GFGIAPANIT DEASFQRYVG LMLAGTDASV RTHAATVLYP
AVFDGSMPYR TQHDRASLLW ADLAASCNTR YLHAAVRTPG YAIEYSVPPA LHLSDTPSVF
YNGPVADPTV NGTIAELLQR QIVRFVKTGN PNGEPDPEVP VYDGRDLLDL GDDGVLVRPD
STDNARCEYW QKVHF
