ID   CUTI_MONFR              Reviewed;         201 AA.
AC   Q8TGB8;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Cutinase;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108};
DE   AltName: Full=Cutin hydrolase;
DE   Flags: Precursor;
GN   Name=CUT1;
OS   Monilinia fructicola (Brown rot fungus) (Ciboria fructicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Monilinia.
OX   NCBI_TaxID=38448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11929215; DOI=10.1006/fgbi.2001.1320;
RA   Wang G.Y., Michailides T.J., Hammock B.D., Lee Y.M., Bostock R.M.;
RT   "Molecular cloning, characterization, and expression of a redox-responsive
RT   cutinase from Monilinia fructicola (Wint.) honey.";
RL   Fungal Genet. Biol. 35:261-276(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (By similarity). Degrades cutin, a
CC       macromolecule that forms the structure of the plant cuticle (By
CC       similarity). Allows pathogenic fungi to penetrate through the cuticular
CC       barrier into the host plant during the initial stage of fungal
CC       infection (By similarity). {ECO:0000250|UniProtKB:P00590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10108};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC   -!- PTM: The 2 disulfide bonds play a critical role in holding the
CC       catalytic residues in juxta-position; reduction of the disulfide
CC       bridges results in the complete inactivation of the enzyme.
CC       {ECO:0000250|UniProtKB:P11373}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; AF305598; AAM10822.1; -; mRNA.
DR   AlphaFoldDB; Q8TGB8; -.
DR   SMR; Q8TGB8; -.
DR   ESTHER; monfr-CUT1; Cutinase.
DR   BRENDA; 3.1.1.74; 3409.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   InterPro; IPR043580; CUTINASE_1.
DR   InterPro; IPR011150; Cutinase_monf.
DR   Pfam; PF01083; Cutinase; 1.
DR   PRINTS; PR00129; CUTINASE.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00155; CUTINASE_1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..201
FT                   /note="Cutinase"
FT                   /id="PRO_0000006444"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   SITE            117
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        31..105
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        164..171
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   201 AA;  20227 MW;  EEA098D9E15019AA CRC64;
     MKTSAQQLLS LLLLPLSAIA APTGEIEARA CSTVTVIFAR GTTETPTLGT VIGPQFLAAL
     KSSFGGSVTM NGVPYAADVP GFLKGGDPTG SKVMANMVSS ALSSCPNTKL VISGYSQGGQ
     LVHNAAKQLP AATTAKIAAA VIFGDPDNGS PVQGVPAAKT KIICHAGDNI CQHGSMILMP
     HLTYGMDATA AAAFVKQVAG S