ID   CUTI1_PENRW             Reviewed;         208 AA.
AC   B6HLS9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable cutinase 1;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10109};
DE   AltName: Full=Cutin hydrolase 1;
DE   Flags: Precursor;
GN   ORFNames=Pc21g21220;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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). {ECO:0000250|UniProtKB:P00590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000255|PROSITE-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; AM920436; CAP97019.1; -; Genomic_DNA.
DR   RefSeq; XP_002569102.1; XM_002569056.1.
DR   AlphaFoldDB; B6HLS9; -.
DR   SMR; B6HLS9; -.
DR   ESTHER; pencw-cuti1; Cutinase.
DR   EnsemblFungi; CAP97019; CAP97019; PCH_Pc21g21220.
DR   GeneID; 8304952; -.
DR   KEGG; pcs:Pc21g21220; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g21220; -.
DR   eggNOG; ENOG502SI38; Eukaryota.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   OMA; KIFCLPT; -.
DR   OrthoDB; 1227171at2759; -.
DR   BioCyc; PCHR:PC21G21220-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
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; 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; PS00931; CUTINASE_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..208
FT                   /note="Probable cutinase 1"
FT                   /id="PRO_5000409922"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10109"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10109"
FT   ACT_SITE        189
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10109"
FT   SITE            48
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            122
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        37..110
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        172..179
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   208 AA;  21906 MW;  DCC68B62C1242455 CRC64;
     MKFSLLALAL ATAAFASPMD IDARALSEGN ELRNGDCKDI TFIFARASTE PGLLILTHPN
     DRMSKPGKVA CQGVGPKYTA DLPSNALPGN TSPAAIAEAQ GLFEQAAKKC PDTQILAGGY
     SQGTAVMDGS IKKLSSDVQA KIKGVALFGY TRNAQERGQI QGFDKDKTKI YCAVGDMVCQ
     GTLVITAAHF TYVADAGAAT RWLVSKLD