ID   CUTI_COLTU              Reviewed;         228 AA.
AC   P10951;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cutinase;
DE            EC=3.1.1.74 {ECO:0000305|PubMed:33606796};
DE   AltName: Full=Cutin hydrolase;
DE   Flags: Precursor;
GN   Name=CUTA;
OS   Colletotrichum truncatum (Anthracnose fungus) (Colletotrichum capsici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum truncatum species complex.
OX   NCBI_TaxID=5467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 48574;
RA   Ettinger W.F., Thukral S.K., Kolattukudy P.E.;
RT   "Structure of cutinase gene, cDNA, and the derived amino acid sequence from
RT   phytopathogenic fungi.";
RL   Biochemistry 26:7883-7892(1987).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=33606796; DOI=10.1371/journal.pone.0247236;
RA   Li Y., Wei J., Yang H., Dai J., Ge X.;
RT   "Molecular dynamics investigation of the interaction between Colletotrichum
RT   capsici cutinase and berberine suggested a mechanism for reduced enzyme
RT   activity.";
RL   PLoS ONE 16:e0247236-e0247236(2021).
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (PubMed:33606796). Degrades cutin, a
CC       macromolecule that forms the structure of the plant cuticle
CC       (PubMed:33606796). Allows pathogenic fungi to penetrate through the
CC       cuticular barrier into the host plant during the initial stage of
CC       fungal infection (By similarity). {ECO:0000250|UniProtKB:P00590,
CC       ECO:0000269|PubMed:33606796}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000305|PubMed:33606796};
CC   -!- ACTIVITY REGULATION: Partially inhibited by berberine; higher
CC       inhibitory effects are observed with longer chain polyester substrates.
CC       {ECO:0000269|PubMed:33606796}.
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:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; M18033; AAA33043.1; -; Genomic_DNA.
DR   PIR; A27451; A27451.
DR   AlphaFoldDB; P10951; -.
DR   SMR; P10951; -.
DR   ESTHER; colca-cutas; Cutinase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA: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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Secreted;
KW   Serine esterase; Signal; Virulence.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..228
FT                   /note="Cutinase"
FT                   /id="PRO_0000006436"
FT   ACT_SITE        140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        208
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            60
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            141
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        49..129
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        191..198
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   228 AA;  23714 MW;  3825D42C23DA139B CRC64;
     MKFLSIISLA VSLVAAAPVE VGLDTGVANL EARQSSTRNE LESGSSSNCP KVIYIFARAS
     TEPGNMGISA GPIVADALES RYGASQVWVQ GVGGPYSADL ASNFIIPEGT SRVAINEAKR
     LFTLANTKCP NSAVVAGGYS QGTAVMASSI SELSSTIQNQ IKGVVLSAIT KNLQNLGRIP
     NFSTSKTEVY CALADAVCYG TLFILPAHFL YQADAATSAP RFLAARIG