CUTI1_FUSVN
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 03-AUG-2022, entry version 137.
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=1.50 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}.
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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 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:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
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 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 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 p-
FT 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
