ID   CUTI_ALTBR              Reviewed;         209 AA.
AC   P41744;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Cutinase;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE   AltName: Full=Cutin hydrolase;
DE   Flags: Precursor;
GN   Name=CUTAB1;
OS   Alternaria brassicicola (Dark leaf spot agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Brassicicola.
OX   NCBI_TaxID=29001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yao C., Koeller W.;
RL   Submitted (NOV-1993) 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, ECO:0000255|PROSITE-
CC         ProRule:PRU10109};
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; U03393; AAA03470.1; -; Unassigned_RNA.
DR   AlphaFoldDB; P41744; -.
DR   SMR; P41744; -.
DR   ESTHER; altbr-cutas; Cutinase.
DR   BRENDA; 3.1.1.74; 9662.
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; IPR043579; CUTINASE_2.
DR   InterPro; IPR011150; Cutinase_monf.
DR   PANTHER; PTHR33630; PTHR33630; 1.
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.
DR   PROSITE; PS00931; CUTINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..209
FT                   /note="Cutinase"
FT                   /id="PRO_0000006432"
FT   ACT_SITE        119
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            40
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            120
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        29..108
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        170..177
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   209 AA;  21649 MW;  1756D06D84093A64 CRC64;
     MMNLNLLLSK PCQASTTRNE LETGSSDACP RTIFIFARGS TEAGNMGALV GPFTANALES
     AYGASNVWVQ GVGGPYTAGL VENALPAGTS QAAIREAQRL FNLAASKCPN TPITAGGYSQ
     GAAVMSNAIP GLSAAVQDQI KGVVLFGYTK NLQNGGRIPN FPTSKTTIYC ETGDLVCNGT
     LIITPAHLLY SDEAAVQAPT FLRAQIDSA