ID   CUTI_FUSSC              Reviewed;         230 AA.
AC   Q99174;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=CUTA;
OS   Fusarium solani subsp. cucurbitae (Neocosmosporum cucurbitae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PGB 153;
RX   PubMed=9100380; DOI=10.1094/mpmi.1997.10.3.355;
RA   Crowhurst R.N., Binnie S.J., Bowen J.K., Hawthorne B.T., Plummer K.M.,
RA   Rees-George J., Rikkerink E.H., Templeton M.D.;
RT   "Effect of disruption of a cutinase gene (cutA) on virulence and tissue
RT   specificity of Fusarium solani f. sp. cucurbitae race 2 toward Cucurbita
RT   maxima and C. moschata.";
RL   Mol. Plant Microbe Interact. 10:355-368(1997).
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; U63335; AAB05922.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q99174; -.
DR   BMRB; Q99174; -.
DR   SMR; Q99174; -.
DR   ESTHER; fusso-cutas; Cutinase.
DR   PHI-base; PHI:2849; -.
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   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..230
FT                   /note="Cutinase"
FT                   /id="PRO_0000006439"
FT   ACT_SITE        136
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        204
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            58
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            137
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        47..125
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        187..194
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   230 AA;  23902 MW;  05FB3C33326405AA CRC64;
     MKFFALTTFL AATASALPTS NPAQELEARQ LGRTTRDDLI NGNSASCADV IFIYARGSTE
     TGNLGTLGPS IASNLESAFG TDGVWIQGVG GAYRATLGDN ALPRGTSSAA IREMLGLFQQ
     ANTKCPDATL IAGGYSQGAA LAAASIEDLD SAIRDKIAGT VLFGYTKNLQ NRGRIPNYPA
     DRTKVFCNVG DLVCTGSLIV AAPHLAYGPD ARGPAPEFLI EKVRAVRGSA