ID   CUTI1_FUSVN             Reviewed;         230 AA.
AC   P00590;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Cutinase 1;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000269|PubMed:18658138, ECO:0000305|PubMed:19810726, ECO:0000305|PubMed:8286366, ECO:0000305|PubMed:8555209};
DE   AltName: Full=Cutin hydrolase 1;
DE   Flags: Precursor;
GN   Name=CUT1; Synonyms=CUTA;
OS   Fusarium vanettenii (Neocosmospora pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 57-94; 113-142 AND
RP   183-192.
RC   STRAIN=T-8;
RX   PubMed=16593482; DOI=10.1073/pnas.81.13.3939;
RA   Soliday C.L., Flurkey W.H., Okita T.W., Kolattukudy P.E.;
RT   "Cloning and structure determination of cDNA for cutinase, an enzyme
RT   involved in fungal penetration of plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:3939-3943(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2703464; DOI=10.1128/jb.171.4.1942-1951.1989;
RA   Soliday C.L., Dickman M.B., Kolattukudy P.E.;
RT   "Structure of the cutinase gene and detection of promoter activity in the
RT   5'-flanking region by fungal transformation.";
RL   J. Bacteriol. 171:1942-1951(1989).
RN   [3]
RP   GLUCURONIC-ACID BINDING AT GLY-32, AND GLYCOSYLATION.
RX   PubMed=7398618; DOI=10.1111/j.1432-1033.1980.tb04580.x;
RA   Lin T.-S., Kolattukudy P.E.;
RT   "Structural studies on cutinase, a glycoprotein containing novel amino
RT   acids and glucuronic acid amide at the N terminus.";
RL   Eur. J. Biochem. 106:341-351(1980).
RN   [4]
RP   FUNCTION.
RX   DOI=10.1038/342446a0;
RA   Dickman M.B., Podila G.K., Kolattukudy P.E.;
RT   "Insertion of cutinase gene into a wound pathogen enables it to infect
RT   intact host.";
RL   Nature 342:446-448(1989).
RN   [5]
RP   BIOTECHNOLOGY.
RX   DOI=10.1002/pola.20684;
RA   Silva C., Carneiro F., O'Neill A., Fonseca L.P., Cabral J.S.M., Guebitz G.,
RA   Cavaco-Paulo A.;
RT   "Cutinase--A new tool for biomodification of synthetic fibers.";
RL   J. Polym. Sci. 128:849-857(2005).
RN   [6]
RP   BIOTECHNOLOGY, AND MUTAGENESIS OF LEU-97; ASN-100; LEU-198; VAL-200 AND
RP   LEU-205.
RX   PubMed=17306400; DOI=10.1016/j.jbiotec.2006.12.028;
RA   Araujo R., Silva C., O'Neill A., Micaelo N., Guebitz G., Soares C.M.,
RA   Casal M., Cavaco-Paulo A.;
RT   "Tailoring cutinase activity towards polyethylene terephthalate and
RT   polyamide 6,6 fibers.";
RL   J. Biotechnol. 128:849-857(2007).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   BIOTECHNOLOGY.
RX   PubMed=18658138; DOI=10.1074/jbc.m800848200;
RA   Chen S., Tong X., Woodard R.W., Du G., Wu J., Chen J.;
RT   "Identification and characterization of bacterial cutinase.";
RL   J. Biol. Chem. 283:25854-25862(2008).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19810726; DOI=10.1021/ja9046697;
RA   Liu Z., Gosser Y., Baker P.J., Ravee Y., Lu Z., Alemu G., Li H.,
RA   Butterfoss G.L., Kong X.P., Gross R., Montclare J.K.;
RT   "Structural and functional studies of Aspergillus oryzae cutinase: enhanced
RT   thermostability and hydrolytic activity of synthetic ester and polyester
RT   degradation.";
RL   J. Am. Chem. Soc. 131:15711-15716(2009).
RN   [9]
RP   ACTIVITY REGULATION, AND BIOTECHNOLOGY.
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).
RN   [10] {ECO:0007744|PDB:1CUS}
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 31-230, ACTIVE SITE, AND
RP   DISULFIDE BONDS.
RX   PubMed=1560844; DOI=10.1038/356615a0;
RA   Martinez C., de Geus P., Lauwereys M., Matthyssens G., Cambillau C.;
RT   "Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine
RT   accessible to solvent.";
RL   Nature 356:615-618(1992).
RN   [11] {ECO:0007744|PDB:2CUT}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 31-228 IN COMPLEX WITH INHIBITOR
RP   PARAOXON, FUNCTION, CATALYTIC ACTIVITY, AND DISULFIDE BONDS.
RX   PubMed=8286366; DOI=10.1021/bi00167a011;
RA   Martinez C., Nicolas A., van Tilbeurgh H., Egloff M.-P., Cudrey C.,
RA   Verger R., Cambillau C.;
RT   "Cutinase, a lipolytic enzyme with a preformed oxyanion hole.";
RL   Biochemistry 33:83-89(1994).
RN   [12] {ECO:0007744|PDB:1XZB, ECO:0007744|PDB:1XZC}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 17-230, AND DISULFIDE BONDS.
RA   Longhi S., Martinez C., Nicolas A., Cambillau C.;
RT   "Core Accessibility of Fusarium Solani Pisi Cutinase Explored by Means of
RT   Hg Derivatives of the S129C Mutant.";
RL   Submitted (NOV-1995) to the PDB data bank.
RN   [13] {ECO:0007744|PDB:1FFA, ECO:0007744|PDB:1FFB, ECO:0007744|PDB:1FFC, ECO:0007744|PDB:1FFD, ECO:0007744|PDB:1FFE}
RP   X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 17-230, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BONDS, AND MUTAGENESIS
RP   OF SER-58 AND ASN-100.
RX   PubMed=8555209; DOI=10.1021/bi9515578;
RA   Nicolas A., Egmond M., Verrips C.T., de Vlieg J., Longhi S., Cambillau C.,
RA   Martinez C.;
RT   "Contribution of cutinase serine 42 side chain to the stabilization of the
RT   oxyanion transition state.";
RL   Biochemistry 35:398-410(1996).
RN   [14] {ECO:0007744|PDB:1CUA, ECO:0007744|PDB:1CUB, ECO:0007744|PDB:1CUC, ECO:0007744|PDB:1CUD, ECO:0007744|PDB:1CUE, ECO:0007744|PDB:1CUF, ECO:0007744|PDB:1CUG, ECO:0007744|PDB:1CUH, ECO:0007744|PDB:1CUI, ECO:0007744|PDB:1CUJ, ECO:0007744|PDB:1CUU}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 17-230 OF MUTANT CYS-136, AND
RP   DISULFIDE BONDS.
RX   PubMed=8990497;
RX   DOI=10.1002/(sici)1097-0134(199612)26:4<442::aid-prot5>3.0.co;2-d;
RA   Longhi S., Nicolas A., Creveld L., Egmond M., Verrips C.T., de Vlieg J.,
RA   Martinez C., Cambillau C.;
RT   "Dynamics of Fusarium solani cutinase investigated through structural
RT   comparison among different crystal forms of its variants.";
RL   Proteins 26:442-458(1996).
RN   [15] {ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1CEX}
RP   X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 17-230, ACTIVE SITE, AND
RP   DISULFIDE BONDS.
RX   PubMed=9175860; DOI=10.1006/jmbi.1997.1000;
RA   Longhi S., Czjzek M., Lamzin V., Nicolas A., Cambillau C.;
RT   "Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase:
RT   stereochemical analysis.";
RL   J. Mol. Biol. 268:779-799(1997).
RN   [16] {ECO:0007744|PDB:1OXM}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-230 IN COMPLEX WITH A
RP   SUBSTRATE ANALOG, AND DISULFIDE BONDS.
RX   PubMed=9041628; DOI=10.1002/pro.5560060202;
RA   Longhi S., Mannesse M., Verheij H.M., De Haas G.H., Egmond M.,
RA   Knoops-Mouthuy E., Cambillau C.;
RT   "Crystal structure of cutinase covalently inhibited by a triglyceride
RT   analogue.";
RL   Protein Sci. 6:275-286(1997).
RN   [17]
RP   STRUCTURE BY NMR.
RX   PubMed=9385640; DOI=10.1002/pro.5560061111;
RA   Prompers J.J., Groenewegen A., van Schaik R.C., Pepermans H.A.M.,
RA   Hilbers C.W.;
RT   "1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase
RT   and preliminary features of the structure in solution.";
RL   Protein Sci. 6:2375-2384(1997).
RN   [18] {ECO:0007744|PDB:3EF3, ECO:0007744|PDB:3ESA, ECO:0007744|PDB:3ESB, ECO:0007744|PDB:3ESC, ECO:0007744|PDB:3ESD}
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 17-230, AND DISULFIDE BONDS.
RX   PubMed=19219875; DOI=10.1002/chem.200801995;
RA   Rutten L., Wieczorek B., Mannie J.P., Kruithof C.A., Dijkstra H.P.,
RA   Egmond M.R., Lutz M., Klein Gebbink R.J., Gros P., van Koten G.;
RT   "Solid-state structural characterization of cutinase-ECE-pincer-metal
RT   hybrids.";
RL   Chemistry 15:4270-4280(2009).
RN   [19] {ECO:0007744|PDB:3QPA, ECO:0007744|PDB:3QPC}
RP   X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 32-228, AND DISULFIDE BONDS.
RA   Lu A., Gosser Y., Montclare J.K., Liu Z., Kong X.;
RT   "Structure of Fusarium Solani Cutinase expressed in Pichia pastoris.";
RL   Submitted (FEB-2011) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (PubMed:18658138, PubMed:8286366,
CC       PubMed:8555209, PubMed:19810726). Degrades cutin, a macromolecule that
CC       forms the structure of the plant cuticle (PubMed:18658138,
CC       PubMed:8286366, PubMed:8555209, PubMed:19810726). Allows pathogenic
CC       fungi to penetrate through the cuticular barrier into the host plant
CC       during the initial stage of fungal infection (Ref.4).
CC       {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726,
CC       ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209,
CC       ECO:0000269|Ref.4}.
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, ECO:0000269|PubMed:18658138,
CC         ECO:0000305|PubMed:19810726, ECO:0000305|PubMed:8286366,
CC         ECO:0000305|PubMed:8555209};
CC   -!- ACTIVITY REGULATION: Inhibited by n-undecyl phosphonate (C11Y4)
CC       (PubMed:25219509). Inhibited by paraoxon (PubMed:8286366,
CC       PubMed:25219509). {ECO:0000269|PubMed:25219509,
CC       ECO:0000269|PubMed:8286366}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.67 uM for p-nitrophenyl acetate (at pH 7.5)
CC         {ECO:0000269|PubMed:19810726};
CC         KM=1.26 uM for p-nitrophenyl butyrate (at pH 7.5)
CC         {ECO:0000269|PubMed:19810726};
CC         KM=0.68 mM for p-nitrophenyl butyrate (at pH 9 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:8555209};
CC         KM=1.48 uM for p-nitrophenyl valerate (at pH 7.5)
CC         {ECO:0000269|PubMed:19810726};
CC         KM=1.5 uM for p-nitrophenyl hexanoate (at pH 7.5)
CC         {ECO:0000269|PubMed:19810726};
CC         Note=kcat is 1800 sec(-1) with p-nitrophenyl butyrate as substrate
CC         (at pH 9 and 30 degrees Celsius). {ECO:0000269|PubMed:8555209};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:18658138};
CC       Temperature dependence:
CC         Optimum temperature is below 30 degrees Celsius (PubMed:19810726).
CC         Optimum temperature is 30-40 degrees Celsius (PubMed:18658138).
CC         {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726};
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   -!- PTM: O-glycosylated; contains one mole each of mannose, arabinose, N-
CC       acetylglucosamine, and glucuronic acid. {ECO:0000269|PubMed:7398618}.
CC   -!- BIOTECHNOLOGY: May have promising applications in chemical and textile
CC       industries as it is capable of hydrolyzing a variety of substrates
CC       including soluble esters and insoluble triglycerides (PubMed:18658138,
CC       PubMed:25219509). Can hydrolyze and thus modulate the surface
CC       properties of synthetic fibers such as the plastic poly(ethylene
CC       terephthalate) (PET), or the textile fibers polyamide 6,6, polyester
CC       and acrylic (Ref.5, PubMed:17306400). {ECO:0000269|PubMed:17306400,
CC       ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:25219509,
CC       ECO:0000269|Ref.5}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; K02640; AAA33334.1; -; mRNA.
DR   EMBL; M29759; AAA33335.1; -; Genomic_DNA.
DR   PIR; A32836; UVFUS.
DR   PDB; 1AGY; X-ray; 1.15 A; A=31-230.
DR   PDB; 1CEX; X-ray; 1.00 A; A=17-230.
DR   PDB; 1CUA; X-ray; 1.80 A; A=17-230.
DR   PDB; 1CUB; X-ray; 1.75 A; A=17-230.
DR   PDB; 1CUC; X-ray; 1.75 A; A=17-230.
DR   PDB; 1CUD; X-ray; 2.70 A; A/B/C=17-230.
DR   PDB; 1CUE; X-ray; 2.10 A; A=33-229.
DR   PDB; 1CUF; X-ray; 1.75 A; A=17-230.
DR   PDB; 1CUG; X-ray; 1.75 A; A=17-230.
DR   PDB; 1CUH; X-ray; 1.75 A; A=17-230.
DR   PDB; 1CUI; X-ray; 2.50 A; A=17-230.
DR   PDB; 1CUJ; X-ray; 1.60 A; A=17-230.
DR   PDB; 1CUS; X-ray; 1.25 A; A=31-230.
DR   PDB; 1CUU; X-ray; 1.69 A; A=17-230.
DR   PDB; 1CUV; X-ray; 2.01 A; A=17-230.
DR   PDB; 1CUW; X-ray; 2.70 A; A/B=17-230.
DR   PDB; 1CUX; X-ray; 1.75 A; A=17-230.
DR   PDB; 1CUY; X-ray; 1.69 A; A=17-230.
DR   PDB; 1CUZ; X-ray; 2.10 A; A=17-230.
DR   PDB; 1FFA; X-ray; 1.69 A; A=17-230.
DR   PDB; 1FFB; X-ray; 1.75 A; A=17-230.
DR   PDB; 1FFC; X-ray; 1.75 A; A=17-230.
DR   PDB; 1FFD; X-ray; 1.69 A; A=17-230.
DR   PDB; 1FFE; X-ray; 1.69 A; A=17-230.
DR   PDB; 1OXM; X-ray; 2.30 A; A/B=17-230.
DR   PDB; 1XZA; X-ray; 1.80 A; A=17-230.
DR   PDB; 1XZB; X-ray; 1.75 A; A=17-230.
DR   PDB; 1XZC; X-ray; 1.75 A; A=17-230.
DR   PDB; 1XZD; X-ray; 2.70 A; A=17-228.
DR   PDB; 1XZE; X-ray; 1.75 A; A=17-230.
DR   PDB; 1XZF; X-ray; 1.69 A; A=17-230.
DR   PDB; 1XZG; X-ray; 1.69 A; A=17-230.
DR   PDB; 1XZH; X-ray; 1.69 A; A=17-230.
DR   PDB; 1XZI; X-ray; 1.69 A; A=17-230.
DR   PDB; 1XZJ; X-ray; 1.69 A; A=17-230.
DR   PDB; 1XZK; X-ray; 2.01 A; A/B=17-230.
DR   PDB; 1XZL; X-ray; 1.69 A; A=17-230.
DR   PDB; 1XZM; X-ray; 1.75 A; A=17-230.
DR   PDB; 2CUT; X-ray; 1.90 A; A=31-228.
DR   PDB; 3EF3; X-ray; 1.50 A; A=17-230.
DR   PDB; 3ESA; X-ray; 2.00 A; A/B=17-230.
DR   PDB; 3ESB; X-ray; 2.30 A; A=17-230.
DR   PDB; 3ESC; X-ray; 1.20 A; A=17-230.
DR   PDB; 3ESD; X-ray; 1.22 A; A=17-230.
DR   PDB; 3QPA; X-ray; 0.85 A; A=32-228.
DR   PDB; 3QPC; X-ray; 0.98 A; A=32-228.
DR   PDBsum; 1AGY; -.
DR   PDBsum; 1CEX; -.
DR   PDBsum; 1CUA; -.
DR   PDBsum; 1CUB; -.
DR   PDBsum; 1CUC; -.
DR   PDBsum; 1CUD; -.
DR   PDBsum; 1CUE; -.
DR   PDBsum; 1CUF; -.
DR   PDBsum; 1CUG; -.
DR   PDBsum; 1CUH; -.
DR   PDBsum; 1CUI; -.
DR   PDBsum; 1CUJ; -.
DR   PDBsum; 1CUS; -.
DR   PDBsum; 1CUU; -.
DR   PDBsum; 1CUV; -.
DR   PDBsum; 1CUW; -.
DR   PDBsum; 1CUX; -.
DR   PDBsum; 1CUY; -.
DR   PDBsum; 1CUZ; -.
DR   PDBsum; 1FFA; -.
DR   PDBsum; 1FFB; -.
DR   PDBsum; 1FFC; -.
DR   PDBsum; 1FFD; -.
DR   PDBsum; 1FFE; -.
DR   PDBsum; 1OXM; -.
DR   PDBsum; 1XZA; -.
DR   PDBsum; 1XZB; -.
DR   PDBsum; 1XZC; -.
DR   PDBsum; 1XZD; -.
DR   PDBsum; 1XZE; -.
DR   PDBsum; 1XZF; -.
DR   PDBsum; 1XZG; -.
DR   PDBsum; 1XZH; -.
DR   PDBsum; 1XZI; -.
DR   PDBsum; 1XZJ; -.
DR   PDBsum; 1XZK; -.
DR   PDBsum; 1XZL; -.
DR   PDBsum; 1XZM; -.
DR   PDBsum; 2CUT; -.
DR   PDBsum; 3EF3; -.
DR   PDBsum; 3ESA; -.
DR   PDBsum; 3ESB; -.
DR   PDBsum; 3ESC; -.
DR   PDBsum; 3ESD; -.
DR   PDBsum; 3QPA; -.
DR   PDBsum; 3QPC; -.
DR   AlphaFoldDB; P00590; -.
DR   BMRB; P00590; -.
DR   SMR; P00590; -.
DR   ChEMBL; CHEMBL2176862; -.
DR   ESTHER; fusso-cutas; Cutinase.
DR   GlyConnect; 116; 2 O-Linked glycans.
DR   GlyCosmos; P00590; No site information, 4 glycans.
DR   VEuPathDB; FungiDB:NECHADRAFT_81019; -.
DR   BRENDA; 3.1.1.74; 8196.
DR   SABIO-RK; P00590; -.
DR   EvolutionaryTrace; P00590; -.
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; alpha/beta hydrolase; 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; PTHR48250:SF3; CUTINASE 1-RELATED; 1.
DR   PANTHER; PTHR48250; CUTINASE 2-RELATED; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   PRINTS; PR00129; CUTINASE.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00155; CUTINASE_1; 1.
DR   PROSITE; PS00931; CUTINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..31
FT                   /evidence="ECO:0000305|PubMed:16593482"
FT                   /id="PRO_0000455280"
FT   CHAIN           32..230
FT                   /note="Cutinase 1"
FT                   /id="PRO_0000006440"
FT   ACT_SITE        136
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0007744|PDB:1AGY"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0007744|PDB:1AGY"
FT   ACT_SITE        204
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0007744|PDB:1AGY"
FT   SITE            58
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209,
FT                   ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY,
FT                   ECO:0007744|PDB:1FFE, ECO:0007744|PDB:1OXM,
FT                   ECO:0007744|PDB:2CUT"
FT   SITE            137
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:9041628,
FT                   ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1OXM,
FT                   ECO:0007744|PDB:2CUT"
FT   MOD_RES         32
FT                   /note="N-D-glucuronoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:7398618"
FT   DISULFID        47..125
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0000269|PubMed:19219875, ECO:0000269|PubMed:8286366,
FT                   ECO:0000269|PubMed:8555209, ECO:0000269|PubMed:8990497,
FT                   ECO:0000269|PubMed:9041628, ECO:0000269|PubMed:9175860,
FT                   ECO:0000269|Ref.12, ECO:0007744|PDB:1AGY,
FT                   ECO:0007744|PDB:1CEX, ECO:0007744|PDB:1CUA,
FT                   ECO:0007744|PDB:1CUB, ECO:0007744|PDB:1CUC,
FT                   ECO:0007744|PDB:1CUD, ECO:0007744|PDB:1CUE,
FT                   ECO:0007744|PDB:1CUF, ECO:0007744|PDB:1CUG,
FT                   ECO:0007744|PDB:1CUH, ECO:0007744|PDB:1CUI,
FT                   ECO:0007744|PDB:1CUJ, ECO:0007744|PDB:1CUS,
FT                   ECO:0007744|PDB:1CUU, ECO:0007744|PDB:1CUV,
FT                   ECO:0007744|PDB:1CUW, ECO:0007744|PDB:1CUX,
FT                   ECO:0007744|PDB:1CUY, ECO:0007744|PDB:1CUZ,
FT                   ECO:0007744|PDB:1FFA, ECO:0007744|PDB:1FFB,
FT                   ECO:0007744|PDB:1FFC, ECO:0007744|PDB:1FFD,
FT                   ECO:0007744|PDB:1FFE, ECO:0007744|PDB:1OXM,
FT                   ECO:0007744|PDB:1XZA, ECO:0007744|PDB:1XZB,
FT                   ECO:0007744|PDB:1XZC, ECO:0007744|PDB:1XZD,
FT                   ECO:0007744|PDB:1XZE, ECO:0007744|PDB:1XZF,
FT                   ECO:0007744|PDB:1XZG, ECO:0007744|PDB:1XZH,
FT                   ECO:0007744|PDB:1XZI, ECO:0007744|PDB:1XZJ,
FT                   ECO:0007744|PDB:1XZK, ECO:0007744|PDB:1XZL,
FT                   ECO:0007744|PDB:1XZM, ECO:0007744|PDB:2CUT,
FT                   ECO:0007744|PDB:3EF3, ECO:0007744|PDB:3ESA,
FT                   ECO:0007744|PDB:3ESB, ECO:0007744|PDB:3ESC,
FT                   ECO:0007744|PDB:3ESD, ECO:0007744|PDB:3QPA,
FT                   ECO:0007744|PDB:3QPC"
FT   DISULFID        187..194
FT                   /evidence="ECO:0000269|PubMed:1560844,
FT                   ECO:0000269|PubMed:19219875, ECO:0000269|PubMed:8286366,
FT                   ECO:0000269|PubMed:8555209, ECO:0000269|PubMed:8990497,
FT                   ECO:0000269|PubMed:9041628, ECO:0000269|PubMed:9175860,
FT                   ECO:0000269|Ref.12, ECO:0007744|PDB:1AGY,
FT                   ECO:0007744|PDB:1CEX, ECO:0007744|PDB:1CUA,
FT                   ECO:0007744|PDB:1CUB, ECO:0007744|PDB:1CUC,
FT                   ECO:0007744|PDB:1CUD, ECO:0007744|PDB:1CUE,
FT                   ECO:0007744|PDB:1CUF, ECO:0007744|PDB:1CUG,
FT                   ECO:0007744|PDB:1CUH, ECO:0007744|PDB:1CUI,
FT                   ECO:0007744|PDB:1CUJ, ECO:0007744|PDB:1CUS,
FT                   ECO:0007744|PDB:1CUU, ECO:0007744|PDB:1CUV,
FT                   ECO:0007744|PDB:1CUW, ECO:0007744|PDB:1CUX,
FT                   ECO:0007744|PDB:1CUY, ECO:0007744|PDB:1CUZ,
FT                   ECO:0007744|PDB:1FFA, ECO:0007744|PDB:1FFB,
FT                   ECO:0007744|PDB:1FFC, ECO:0007744|PDB:1FFD,
FT                   ECO:0007744|PDB:1FFE, ECO:0007744|PDB:1OXM,
FT                   ECO:0007744|PDB:1XZA, ECO:0007744|PDB:1XZB,
FT                   ECO:0007744|PDB:1XZC, ECO:0007744|PDB:1XZD,
FT                   ECO:0007744|PDB:1XZE, ECO:0007744|PDB:1XZF,
FT                   ECO:0007744|PDB:1XZG, ECO:0007744|PDB:1XZH,
FT                   ECO:0007744|PDB:1XZI, ECO:0007744|PDB:1XZJ,
FT                   ECO:0007744|PDB:1XZK, ECO:0007744|PDB:1XZL,
FT                   ECO:0007744|PDB:1XZM, ECO:0007744|PDB:2CUT,
FT                   ECO:0007744|PDB:3EF3, ECO:0007744|PDB:3ESA,
FT                   ECO:0007744|PDB:3ESB, ECO:0007744|PDB:3ESC,
FT                   ECO:0007744|PDB:3ESD, ECO:0007744|PDB:3QPA,
FT                   ECO:0007744|PDB:3QPC"
FT   MUTAGEN         58
FT                   /note="S->A: Severely decreases activity on p-nitrophenyl
FT                   butyrate."
FT                   /evidence="ECO:0000269|PubMed:8555209"
FT   MUTAGEN         97
FT                   /note="L->A: Increases activity on p-nitrophenyl butyrate."
FT                   /evidence="ECO:0000269|PubMed:17306400"
FT   MUTAGEN         100
FT                   /note="N->A,L,D,W: Severely decreases activity on
FT                   p-nitrophenyl butyrate."
FT                   /evidence="ECO:0000269|PubMed:17306400,
FT                   ECO:0000269|PubMed:8555209"
FT   MUTAGEN         100
FT                   /note="N->A: Increases activity on poly(ethylene
FT                   terephthalate) (PET) and decreases activity on polyamide
FT                   6,6."
FT                   /evidence="ECO:0000269|PubMed:17306400"
FT   MUTAGEN         198
FT                   /note="L->A: Increases activity on p-nitrophenyl butyrate,
FT                   poly(ethylene terephthalate) (PET) and polyamide 6,6."
FT                   /evidence="ECO:0000269|PubMed:17306400"
FT   MUTAGEN         200
FT                   /note="V->A: Increases activity on p-nitrophenyl butyrate
FT                   and poly(ethylene terephthalate) (PET)."
FT                   /evidence="ECO:0000269|PubMed:17306400"
FT   MUTAGEN         205
FT                   /note="L->A: Increases activity on p-nitrophenyl butyrate
FT                   and decreases activity on poly(ethylene terephthalate)
FT                   (PET)."
FT                   /evidence="ECO:0000269|PubMed:17306400"
FT   CONFLICT        48
FT                   /note="R -> A (in Ref. 2; AAA33335)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="R -> A (in Ref. 2; AAA33335)"
FT                   /evidence="ECO:0000305"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:1CEX"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   TURN            62..67
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           97..101
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           108..124
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           138..148
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   STRAND          157..164
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   TURN            166..173
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           192..195
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           208..212
FT                   /evidence="ECO:0007829|PDB:3QPA"
FT   HELIX           214..227
FT                   /evidence="ECO:0007829|PDB:3QPA"
SQ   SEQUENCE   230 AA;  23982 MW;  7253ACAA657AD1AB CRC64;
     MKFFALTTLL AATASALPTS NPAQELEARQ LGRTTRDDLI NGNSASCRDV IFIYARGSTE
     TGNLGTLGPS IASNLESAFG KDGVWIQGVG GAYRATLGDN ALPRGTSSAA IREMLGLFQQ
     ANTKCPDATL IAGGYSQGAA LAAASIEDLD SAIRDKIAGT VLFGYTKNLQ NRGRIPNYPA
     DRTKVFCNTG DLVCTGSLIV AAPHLAYGPD ARGPAPEFLI EKVRAVRGSA
//