CUTI2_PENRW
ID CUTI2_PENRW Reviewed; 212 AA.
AC B6H2E9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Probable cutinase 2;
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Cutin hydrolase 2;
DE Flags: Precursor;
GN ORFNames=Pc13g05110;
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:PRU10108, ECO:0000255|PROSITE-
CC ProRule:PRU10109};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AM920428; CAP91580.1; -; Genomic_DNA.
DR RefSeq; XP_002558946.1; XM_002558900.1.
DR AlphaFoldDB; B6H2E9; -.
DR SMR; B6H2E9; -.
DR ESTHER; pencw-cuti2; Cutinase.
DR EnsemblFungi; CAP91580; CAP91580; PCH_Pc13g05110.
DR GeneID; 8312382; -.
DR KEGG; pcs:Pc13g05110; -.
DR VEuPathDB; FungiDB:PCH_Pc13g05110; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR OMA; SCPKAIF; -.
DR OrthoDB; 1227171at2759; -.
DR BioCyc; PCHR:PC13G05110-MON; -.
DR Proteomes; UP000000724; Contig Pc00c13.
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; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..212
FT /note="Probable cutinase 2"
FT /id="PRO_5000408953"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 180
FT /evidence="ECO:0000250|UniProtKB:A0A2J8C362"
FT ACT_SITE 193
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 47
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 36..114
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 62..75
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 176..183
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 212 AA; 22229 MW; 10F4139BF8F0C925 CRC64;
MNFKLLSLLL AGLATAGPIE QRQTSSSGNE LRDGPCQPVT FIFARASTEQ GLLGGSTGPA
VCNDLKSARN QEVACQGVGP KYQATLAANS LPAGTSDEAI EEAKGLFEQA ASKCPDTQIV
AGGYSQGTAV MHGAIPKLSD AIKDQIKGVV LFGDTRNQQD NEQIPDFPKD KTKIYCAVGD
QVCHGSLIVA APHFSYVADA GDASRFLVEK LD
