CUTI1_HYPJR
ID CUTI1_HYPJR Reviewed; 248 AA.
AC A0A024SC78;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Cutinase {ECO:0000255|RuleBase:RU361263};
DE EC=3.1.1.74 {ECO:0000255|RuleBase:RU361263, ECO:0000269|PubMed:25219509};
DE Flags: Precursor;
GN ORFNames=M419DRAFT_76732 {ECO:0000312|EMBL:ETS02914.1};
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414 {ECO:0000312|Proteomes:UP000024376};
RN [1] {ECO:0000312|Proteomes:UP000024376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30
RC {ECO:0000312|Proteomes:UP000024376};
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
RN [2] {ECO:0007744|PDB:4PSC, ECO:0007744|PDB:4PSD, ECO:0007744|PDB:4PSE}
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 31-248, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MASS
RP SPECTROMETRY, ACTIVE SITE, AND DISULFIDE BONDS.
RX PubMed=25219509; DOI=10.1016/j.jmb.2014.09.003;
RA Roussel A., Amara S., Nyyssola A., Mateos-Diaz E., Blangy S., Kontkanen H.,
RA Westerholm-Parvinen A., Carriere F., Cambillau C.;
RT "A Cutinase from Trichoderma reesei with a lid-covered active site and
RT kinetic properties of true lipases.";
RL J. Mol. Biol. 426:3757-3772(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:25219509). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle
CC (PubMed:25219509). {ECO:0000269|PubMed:25219509}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000269|PubMed:25219509};
CC -!- ACTIVITY REGULATION: Weakly inhibited by n-undecyl phosphonate (C11Y4)
CC (PubMed:25219509). Activity unaffected by paraoxon (PubMed:25219509).
CC {ECO:0000269|PubMed:25219509}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-7. {ECO:0000269|PubMed:25219509};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}.
CC -!- DOMAIN: In contract to classical cutinases, possesses a lid formed by
CC two N-terminal helices which covers its active site (PubMed:25219509).
CC The lid opens in the presence of surfactants to uncover the catalytic
CC crevice, allowing enzyme activity and inhibition (PubMed:25219509).
CC {ECO:0000269|PubMed:25219509}.
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=23748; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25219509};
CC -!- SIMILARITY: Belongs to the cutinase family.
CC {ECO:0000255|RuleBase:RU361263}.
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DR EMBL; KI911144; ETS02914.1; -; Genomic_DNA.
DR PDB; 4PSC; X-ray; 1.15 A; A=1-204.
DR PDB; 4PSD; X-ray; 1.52 A; A=1-204.
DR PDB; 4PSE; X-ray; 1.71 A; A/B=1-204.
DR PDBsum; 4PSC; -.
DR PDBsum; 4PSD; -.
DR PDBsum; 4PSE; -.
DR EnsemblFungi; ETS02914; ETS02914; M419DRAFT_76732.
DR KEGG; trr:M419DRAFT_76732; -.
DR HOGENOM; CLU_040058_2_1_1; -.
DR OrthoDB; 1193797at2759; -.
DR Proteomes; UP000024376; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 3D-structure; Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..28
FT /evidence="ECO:0000269|PubMed:25219509"
FT /id="PRO_0000455277"
FT CHAIN 29..248
FT /note="Cutinase"
FT /evidence="ECO:0000305"
FT /id="PRO_5005101809"
FT REGION 31..70
FT /note="Lid covering the active site of the uncomplexed
FT enzyme"
FT /evidence="ECO:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSC, ECO:0007744|PDB:4PSD"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSE"
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:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSE"
FT SITE 165
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSE"
FT DISULFID 55..91
FT /evidence="ECO:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSC, ECO:0007744|PDB:4PSD,
FT ECO:0007744|PDB:4PSE"
FT DISULFID 79..153
FT /evidence="ECO:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSC, ECO:0007744|PDB:4PSD,
FT ECO:0007744|PDB:4PSE"
FT DISULFID 212..219
FT /evidence="ECO:0000269|PubMed:25219509,
FT ECO:0007744|PDB:4PSC, ECO:0007744|PDB:4PSD,
FT ECO:0007744|PDB:4PSE"
SQ SEQUENCE 248 AA; 25924 MW; 1FE2B82328641D42 CRC64;
MRSLAILTTL LAGHAFAYPK PAPQSVNRRD WPSINEFLSE LAKVMPIGDT ITAACDLISD
GEDAAASLFG ISETENDPCG DVTVLFARGT CDPGNVGVLV GPWFFDSLQT ALGSRTLGVK
GVPYPASVQD FLSGSVQNGI NMANQIKSVL QSCPNTKLVL GGYSQGSMVV HNAASNLDAA
TMSKISAVVL FGDPYYGKPV ANFDAAKTLV VCHDGDNICQ GGDIILLPHL TYAEDADTAA
AFVVPLVS
