CUTI1_TRIHA
ID CUTI1_TRIHA Reviewed; 248 AA.
AC A8QPD8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Cutinase cut1 {ECO:0000303|PubMed:18987860};
DE EC=3.1.1.74 {ECO:0000305|PubMed:18987860};
DE AltName: Full=Thcut1 {ECO:0000303|PubMed:18987860};
DE Flags: Precursor;
GN Name=cut1 {ECO:0000303|PubMed:18987860};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000312|EMBL:ABN48556.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150
RC {ECO:0000303|PubMed:18987860};
RX PubMed=18987860; DOI=10.1007/s00294-008-0218-6;
RA Rubio M.B., Cardoza R.E., Hermosa R., Gutierrez S., Monte E.;
RT "Cloning and characterization of the Thcut1 gene encoding a cutinase of
RT Trichoderma harzianum T34.";
RL Curr. Genet. 54:301-312(2008).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:18987860). May degrade cutin,
CC a macromolecule that forms the structure of the plant cuticle
CC (PubMed:18987860). May also degrade suberin, a specialized
CC macromolecule found in the cell wall of various plant tissues
CC (PubMed:18987860). {ECO:0000269|PubMed:18987860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000305|PubMed:18987860};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for p-nitrophenyl acetate (at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:18987860};
CC KM=0.57 mM for p-nitrophenyl butyrate (at pH 8 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:18987860};
CC KM=0.82 mM for p-nitrophenyl valerate (at pH 8 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:18987860};
CC KM=0.085 mM for p-nitrophenyl palmitate (at pH 8 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:18987860};
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:18987860};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18987860}.
CC -!- INDUCTION: Induced during growth on olive oil (PubMed:18987860).
CC Induced during growth on the lipidic carbon source 16-
CC hydroxyhexadecanoic acid (synthetic cutin monomer) (PubMed:18987860).
CC Induced during growth on plant material (PubMed:18987860). Induced
CC during growth on pectin (PubMed:18987860). Repressed during growth on
CC glucose carbon source (PubMed:18987860). {ECO:0000269|PubMed:18987860}.
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; EF108302; ABN48556.1; -; Genomic_DNA.
DR ESTHER; triha-a8qpd8; Cutinase.
DR BRENDA; 3.1.1.74; 6445.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-UniRule.
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.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|RuleBase:RU361263"
FT CHAIN 18..248
FT /note="Cutinase cut1"
FT /evidence="ECO:0000255|RuleBase:RU361263"
FT /id="PRO_5005117511"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 216
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 229
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 90
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 165
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 79..153
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 212..219
FT /evidence="ECO:0000250|UniProtKB:P00590"
SQ SEQUENCE 248 AA; 26007 MW; 3CDEF12D896F9DE6 CRC64;
MRSLSLFTAL LAGQAFAYPK PVLQSSTRRD WPTINEFLTE LAEIMPIGDT VSAACDLIGD
AEDVAADLFD ISNTENDACG DVTVLFARGT CDPGNVGVLV GPWFFNSLET ALPNKKVGVK
GVPYPASVQG FLSGSVQPGI DMANQIKSVI SSCPNTKLVL GGYSQGSMVV HNAASNLDAA
TMAKVSAVVL FGDPYDGRPV ANYDASKVLV VCHDGDNICQ GGDFILLPHL TYAEDADTAA
AFVKPLVS
