CUTI_DIDRA
ID CUTI_DIDRA Reviewed; 223 AA.
AC P29292;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=CUT;
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CBS 534.65;
RA Tenhaken R., Barz W.;
RL Submitted (APR-1992) 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; X65628; CAA46582.1; -; Genomic_DNA.
DR PIR; S21427; S21427.
DR AlphaFoldDB; P29292; -.
DR SMR; P29292; -.
DR ESTHER; ascra-cutas; 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; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..223
FT /note="Cutinase"
FT /id="PRO_0000006433"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 189
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 202
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 57
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 136
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 46..124
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 185..192
FT /evidence="ECO:0000250|UniProtKB:P00590"
SQ SEQUENCE 223 AA; 23520 MW; 1E82A5ADD1B5E7FB CRC64;
MKFFAFSMLI GEASPIVLAL RRTTLEVRQL DPIIRSELEQ GSSSSCPKAI LIFARGSTEI
GNMGVSAGPA VASALEAYGA DQIWVQGVGG PYTADLPSNF LPGGTSQSAI NEAVRLFNEA
NTKCPSTPIV AGGYSQGTAV MAGAIPKLDA VRARVVGTVL FGYTQNQQNN KGIKDYPQED
LQVYCEVGDL VCDGTLIITV SHFLYLEEAA GPAPEFLKSK IGA
