ID   CUTI_BLUHO              Reviewed;         236 AA.
AC   Q8X1P1;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 59.
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   Blumeria hordei (Barley powdery mildew) (Blumeria graminis f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=2867405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang Z., Perfect E., Gurr S.J.;
RT   "Cutinase gene isolation and functional analysis from Blumeria graminis
RT   during the barley/powdery mildew interactions.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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; AF326784; AAL67672.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X1P1; -.
DR   SMR; Q8X1P1; -.
DR   ESTHER; blugr-CUT1; Cutinase.
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   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..236
FT                   /note="Cutinase"
FT                   /id="PRO_0000006438"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        218
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   SITE            155
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        66..143
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        202..209
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   236 AA;  24604 MW;  6528C4F26A4AFCEC CRC64;
     MSLTLFSFLS LVSILCIVTA APVTNVNFTS IQVSSMQHIA AINKASFFSP TALPANATEN
     GLTGSCKPII LIFAKGTGEN GNVGDGSSPG PAWFSELRNA IGEDKIAVQG VQYEADVFGY
     LVGGDPEGSQ NYLTITNQAV TQCPNSKIVI GGYSQGAQIT HNAAQLYSPL VTSRIAAVVL
     FGDPYTDKPV GQVSPSSVLE ICHDGDIICT GSGGPDPHLT YSKNATCAAK FVLDRI