CUTI_BOTFU
ID CUTI_BOTFU Reviewed; 202 AA.
AC Q00298;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cutinase;
DE EC=3.1.1.74 {ECO:0000305|PubMed:9002270};
DE AltName: Full=Cutin hydrolase;
DE Flags: Precursor;
GN Name=cutA {ECO:0000303|PubMed:9002269};
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=SAS56;
RX PubMed=9002269; DOI=10.1094/mpmi.1997.10.1.21;
RA van der Vlugt-Bergmans C.J.B., Wagemakers L.C.A.M., van Kan J.A.L.;
RT "Cloning and expression of the cutinase A gene of Botrytis cinerea.";
RL Mol. Plant Microbe Interact. 10:21-29(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9002270; DOI=10.1094/mpmi.1997.10.1.30;
RA van Kan J.A., van't Klooster J.W., Wagemakers C.A., Dees D.C.,
RA van der Vlugt-Bergmans C.J.;
RT "Cutinase A of Botrytis cinerea is expressed, but not essential, during
RT penetration of gerbera and tomato.";
RL Mol. Plant Microbe Interact. 10:30-38(1997).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:9002270). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle
CC (PubMed:9002270). 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:9002270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000305|PubMed:9002270};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC -!- INDUCTION: Induced during infection (PubMed:9002269, PubMed:9002270).
CC By contact with cutin (PubMed:9002269, PubMed:9002270). Repressed by
CC glucose (PubMed:9002269, PubMed:9002270). {ECO:0000269|PubMed:9002269,
CC ECO:0000269|PubMed:9002270}.
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 -!- DISRUPTION PHENOTYPE: Decreases cellular carboxylic ester hydrolase
CC activity (PubMed:9002270). Does not affect penetration of the cuticle
CC of gerbera flowers or tomato fruit (PubMed:9002270).
CC {ECO:0000269|PubMed:9002270}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; Z69264; CAA93255.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00298; -.
DR SMR; Q00298; -.
DR ESTHER; botci-cutas; Cutinase.
DR ABCD; Q00298; 1 sequenced antibody.
DR OMA; TYPMDGS; -.
DR BRENDA; 3.1.1.74; 918.
DR PHI-base; PHI:69; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IMP: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 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 Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..202
FT /note="Cutinase"
FT /id="PRO_0000006435"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 169
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 182
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 31..106
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 165..172
FT /evidence="ECO:0000250|UniProtKB:P00590"
SQ SEQUENCE 202 AA; 20253 MW; 031D64725A23D8E7 CRC64;
MKTSAQQLLS ALLLPLSVLA APTGSIEARA CSDVTVIFAR GTTETGTLGT VVGPPFLAAL
KSALGSSSVT MNGVDYPADV PGFLQGGDPA GSQTMATMVT STLSSCPDTK LVISGYSQGG
QLVHNAAKLL PAETTAKISS AVIFGDPDNG DPVQGVSADR TDIICHAGDN ICQGGSLILL
AHLTYGMDTT AAAAFVKKAA GL
