ID   CUTI1_COPCI             Reviewed;         199 AA.
AC   B9U443;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Cutinase CUT1 {ECO:0000303|PubMed:19201950};
DE            EC=3.1.1.74 {ECO:0000269|PubMed:19201950};
DE   AltName: Full=CcCUT1 {ECO:0000303|PubMed:19201950};
DE   Flags: Precursor;
GN   Name=CUT1 {ECO:0000303|PubMed:19201950};
GN   Synonyms=09668 {ECO:0000303|PubMed:19201950};
OS   Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=5346 {ECO:0000312|EMBL:ACB87560.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, AND PYROGLUTAMATE
RP   FORMATION AT GLN-28.
RC   STRAIN=VTT D-041011 {ECO:0000312|EMBL:ACB87560.1};
RX   PubMed=19201950; DOI=10.1128/aem.02103-08;
RA   Kontkanen H., Westerholm-Parvinen A., Saloheimo M., Bailey M., Ratto M.,
RA   Mattila I., Mohsina M., Kalkkinen N., Nakari-Setala T., Buchert J.;
RT   "Novel Coprinopsis cinerea polyesterase that hydrolyzes cutin and
RT   suberin.";
RL   Appl. Environ. Microbiol. 75:2148-2157(2009).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=19739639; DOI=10.1021/jf9008907;
RA   Jaervinen R., Silvestre A.J., Holopainen U., Kaimainen M., Nyyssoelae A.,
RA   Gil A.M., Pascoal Neto C., Lehtinen P., Buchert J., Kallio H.;
RT   "Suberin of potato (Solanum tuberosum var. Nikola): comparison of the
RT   effect of cutinase CcCut1 with chemical depolymerization.";
RL   J. Agric. Food Chem. 57:9016-9027(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (PubMed:19201950, PubMed:19739639).
CC       Degrades cutin, a macromolecule that forms the structure of the plant
CC       cuticle (PubMed:19201950). Also degrades suberin, a specialized
CC       macromolecule found in the cell wall of various plant tissues
CC       (PubMed:19201950, PubMed:19739639). {ECO:0000269|PubMed:19201950,
CC       ECO:0000269|PubMed:19739639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000269|PubMed:19201950};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-8. {ECO:0000269|PubMed:19201950};
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   -!- MASS SPECTROMETRY: Mass=18863; Method=Electrospray; Note=The mass
CC       corresponds to protein with a C-terminal six histidine tag and two
CC       disulfide bridges.; Evidence={ECO:0000269|PubMed:19201950};
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; EU435153; ACB87560.1; -; Genomic_DNA.
DR   SMR; B9U443; -.
DR   ESTHER; copci-b9u443; Cutinase.
DR   VEuPathDB; FungiDB:CC1G_09668; -.
DR   VEuPathDB; FungiDB:CC2G_003771; -.
DR   OMA; GAHVNSM; -.
DR   BRENDA; 3.1.1.74; 1606.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0050525; F:cutinase activity; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   InterPro; IPR011150; Cutinase_monf.
DR   Pfam; PF01083; Cutinase; 1.
DR   PRINTS; PR00129; CUTINASE.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Pyrrolidone carboxylic acid; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..27
FT                   /evidence="ECO:0000269|PubMed:19201950"
FT                   /id="PRO_0000455276"
FT   CHAIN           28..199
FT                   /note="Cutinase CUT1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002892738"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            117
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   MOD_RES         28
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:19201950"
FT   DISULFID        31..105
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        164..171
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   199 AA;  20805 MW;  2A25CEC3C6E46D2A CRC64;
     MKFTTLATLA LGAVSALAAP VTELESRQLF CRDVYVFFAR GTGEVGTLGT VVGPGLSAAV
     KLAVRDSVEF EGIDYPALVS GYLAGGDRGG ARTMANKVSQ TASRCPNAKI FISGYSQGAQ
     VTHLAARQLS AADQARVTGV VTFGDPYRDD ALPGGLQSRR KTYCNVGDLI CAGLPTLLAP
     HFTYGSDTPD AARWIAARV