PETH_IDESA
ID PETH_IDESA Reviewed; 290 AA.
AC A0A0K8P6T7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Poly(ethylene terephthalate) hydrolase {ECO:0000303|PubMed:26965627, ECO:0000303|PubMed:29235460, ECO:0000303|PubMed:29666242};
DE Short=PET hydrolase {ECO:0000303|PubMed:26965627, ECO:0000303|PubMed:29235460, ECO:0000303|PubMed:29666242};
DE Short=PETase {ECO:0000303|PubMed:26965627, ECO:0000303|PubMed:29235460, ECO:0000303|PubMed:29666242};
DE EC=3.1.1.101 {ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29235460, ECO:0000269|PubMed:29374183, ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242};
DE AltName: Full=PET-digesting enzyme {ECO:0000303|PubMed:29666242};
DE Flags: Precursor;
GN ORFNames=ISF6_4831 {ECO:0000312|EMBL:GAP38373.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Ideonella.
OX NCBI_TaxID=1547922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION BY
RP PET, PATHWAY, AND BIOTECHNOLOGY.
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6;
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32269349; DOI=10.1038/s41586-020-2149-4;
RA Tournier V., Topham C.M., Gilles A., David B., Folgoas C., Moya-Leclair E.,
RA Kamionka E., Desrousseaux M.L., Texier H., Gavalda S., Cot M., Guemard E.,
RA Dalibey M., Nomme J., Cioci G., Barbe S., Chateau M., Andre I.,
RA Duquesne S., Marty A.;
RT "An engineered PET depolymerase to break down and recycle plastic
RT bottles.";
RL Nature 580:216-219(2020).
RN [3] {ECO:0007744|PDB:5XFY, ECO:0007744|PDB:5XFZ, ECO:0007744|PDB:5XG0, ECO:0007744|PDB:5XH2, ECO:0007744|PDB:5XH3}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 30-290 OF WILD-TYPE AND MUTANTS
RP ALA-160 AND GLY-132/ALA-160 IN COMPLEXES WITH PARA-NITROPHENOL AND
RP 1-(2-HYDROXYETHYL)-4-METHYLTEREPHTHALATE (HEMT), DISULFIDE BOND, FUNCTION,
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=29235460; DOI=10.1038/s41467-017-02255-z;
RA Han X., Liu W., Huang J.W., Ma J., Zheng Y., Ko T.P., Xu L., Cheng Y.S.,
RA Chen C.C., Guo R.T.;
RT "Structural insight into catalytic mechanism of PET hydrolase.";
RL Nat. Commun. 8:2106-2106(2017).
RN [4] {ECO:0007744|PDB:6ANE}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 29-290, DISULFIDE BOND, AND
RP SUBSTRATE DOCKING.
RX PubMed=29590588; DOI=10.1016/j.bpj.2018.02.005;
RA Fecker T., Galaz-Davison P., Engelberger F., Narui Y., Sotomayor M.,
RA Parra L.P., Ramirez-Sarmiento C.A.;
RT "Active site flexibility as a hallmark for efficient PET degradation by I.
RT sakaiensis PETase.";
RL Biophys. J. 114:1302-1312(2018).
RN [5] {ECO:0007744|PDB:5YFE}
RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 27-290, SUBSTRATE DOCKING,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP MUTAGENESIS OF TYR-87; GLN-119; TRP-159; SER-160; MET-161; TRP-185;
RP ASP-206; SER-214 AND HIS-237, AND DISULFIDE BOND.
RX PubMed=29603535; DOI=10.1002/cbic.201800097;
RA Liu B., He L., Wang L., Li T., Li C., Liu H., Luo Y., Bao R.;
RT "Protein crystallography and site-direct mutagenesis analysis of the
RT poly(ethylene terephthalate) hydrolase PETase from Ideonella sakaiensis.";
RL ChemBioChem 19:1471-1475(2018).
RN [6] {ECO:0007744|PDB:5XJH, ECO:0007744|PDB:5YNS}
RP X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 34-290 OF WILD-TYPE AND MUTANT
RP ALA-280, DISULFIDE BOND, SUBSTRATE DOCKING, FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF TYR-87; TRP-159; SER-160; TRP-185;
RP CYS-203; ASP-206; HIS-237; SER-238; CYS-239; ASN-241 AND ARG-280.
RX PubMed=29374183; DOI=10.1038/s41467-018-02881-1;
RA Joo S., Cho I.J., Seo H., Son H.F., Sagong H.Y., Shin T.J., Choi S.Y.,
RA Lee S.Y., Kim K.J.;
RT "Structural insight into molecular mechanism of poly(ethylene
RT terephthalate) degradation.";
RL Nat. Commun. 9:382-382(2018).
RN [7] {ECO:0007744|PDB:6EQD, ECO:0007744|PDB:6EQE, ECO:0007744|PDB:6EQF, ECO:0007744|PDB:6EQG, ECO:0007744|PDB:6EQH}
RP X-RAY CRYSTALLOGRAPHY (0.92 ANGSTROMS), SUBSTRATE DOCKING, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOTECHNOLOGY, ACTIVE SITE,
RP DISULFIDE BOND, AND MUTAGENESIS OF TRP-159; TRP-185 AND SER-238.
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6;
RX PubMed=29666242; DOI=10.1073/pnas.1718804115;
RA Austin H.P., Allen M.D., Donohoe B.S., Rorrer N.A., Kearns F.L.,
RA Silveira R.L., Pollard B.C., Dominick G., Duman R., El Omari K.,
RA Mykhaylyk V., Wagner A., Michener W.E., Amore A., Skaf M.S., Crowley M.F.,
RA Thorne A.W., Johnson C.W., Woodcock H.L., McGeehan J.E., Beckham G.T.;
RT "Characterization and engineering of a plastic-degrading aromatic
RT polyesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E4350-E4357(2018).
RN [8] {ECO:0007744|PDB:6IJ3, ECO:0007744|PDB:6IJ4, ECO:0007744|PDB:6IJ5, ECO:0007744|PDB:6IJ6}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 34-290 OF MUTANTS
RP ASP-121/HIS-186; GLU-121/HIS-186; ALA-181 AND GLU-121/HIS-186/ALA-280,
RP DISULFIDE BOND, PROTEIN ENGINEERING, AND MUTAGENESIS OF SER-121; ASP-186
RP AND ARG-280.
RX DOI=10.1021/acscatal.9b00568;
RA Son H.F., Cho I.J., Joo S., Seo H., Sagong H.Y., Choi S.Y., Lee S.Y.,
RA Kim K.J.;
RT "Rational Protein Engineering of Thermo-Stable PETase from Ideonella
RT sakaiensis for Highly Efficient PET Degradation.";
RL ACS Catal. 9:3519-3526(2019).
RN [9] {ECO:0007744|PDB:6ILW, ECO:0007744|PDB:6ILX}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 28-290 OF WILD-TYPE AND MUTANT
RP PHE-159, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND, AND MUTAGENESIS OF SER-93;
RP TRP-159 AND ASN-241.
RX PubMed=30502092; DOI=10.1016/j.bbrc.2018.11.148;
RA Liu C., Shi C., Zhu S., Wei R., Yin C.C.;
RT "Structural and functional characterization of polyethylene terephthalate
RT hydrolase from Ideonella sakaiensis.";
RL Biochem. Biophys. Res. Commun. 508:289-294(2019).
RN [10] {ECO:0007744|PDB:6QGC}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=30979881; DOI=10.1038/s41467-019-09326-3;
RA Palm G.J., Reisky L., Bottcher D., Muller H., Michels E.A.P., Walczak M.C.,
RA Berndt L., Weiss M.S., Bornscheuer U.T., Weber G.;
RT "Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a
RT substrate.";
RL Nat. Commun. 10:1717-1717(2019).
CC -!- FUNCTION: Involved in the degradation and assimilation of the plastic
CC poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use
CC PET as its major energy and carbon source for growth. Likely acts
CC synergistically with MHETase to depolymerize PET (PubMed:26965627).
CC Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl)
CC terephthalate (MHET) as the major product (PubMed:26965627,
CC PubMed:32269349, PubMed:29666242, PubMed:29603535, PubMed:29374183,
CC PubMed:29235460). Also depolymerizes another semiaromatic polyester,
CC poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging,
CC bioderived PET replacement with improved gas barrier properties
CC (PubMed:29666242). In contrast, PETase does not degrade aliphatic
CC polyesters such as polylactic acid (PLA) and polybutylene succinate
CC (PBS) (PubMed:29666242). Is also able to hydrolyze bis(hydroxyethyl)
CC terephthalate (BHET) to yield MHET with no further decomposition, but
CC terephthalate (TPA) can also be observed (PubMed:26965627,
CC PubMed:29603535, PubMed:29374183). Shows esterase activity towards p-
CC nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro
CC (PubMed:26965627, PubMed:30502092). {ECO:0000269|PubMed:26965627,
CC ECO:0000269|PubMed:29235460, ECO:0000269|PubMed:29374183,
CC ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242,
CC ECO:0000269|PubMed:30502092, ECO:0000269|PubMed:32269349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(ethylene terephthalate)(n) + H2O = (ethylene
CC terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+);
CC Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701,
CC ChEBI:CHEBI:131704; EC=3.1.1.101;
CC Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29235460,
CC ECO:0000269|PubMed:29374183, ECO:0000269|PubMed:29603535,
CC ECO:0000269|PubMed:29666242, ECO:0000269|PubMed:32269349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000269|PubMed:26965627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2,5-ethylene furandicarboxylate)(n) + 2 H2O = (2,5-ethylene
CC furandicarboxylate)(n-1) + 2,5-dicarboxyfuran + ethylene glycol + 2
CC H(+); Xref=Rhea:RHEA:42648, Rhea:RHEA-COMP:14671, Rhea:RHEA-
CC COMP:14672, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30742,
CC ChEBI:CHEBI:83389, ChEBI:CHEBI:140646;
CC Evidence={ECO:0000269|PubMed:29666242};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622;
CC Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) +
CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656;
CC Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30502092};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:30502092};
CC -!- ACTIVITY REGULATION: Salts and glycerol enhance the enzymatic activity
CC in vitro towards pNP-esters, while detergents and organic solvents
CC reduce the enzymatic activity. {ECO:0000269|PubMed:30502092}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.431 mM for pNP-acetate {ECO:0000269|PubMed:30502092};
CC KM=0.315 mM for pNP-butanoate {ECO:0000269|PubMed:30502092};
CC KM=0.053 mM for pNP-hexanoate {ECO:0000269|PubMed:30502092};
CC KM=0.048 mM for pNP-octanoate {ECO:0000269|PubMed:30502092};
CC KM=2.283 mM for pNP-dodecanoate {ECO:0000269|PubMed:30502092};
CC Note=kcat is 1590 sec(-1) for the hydrolysis of pNP-acetate. kcat is
CC 1353 sec(-1) for the hydrolysis of pNP-butanoate. kcat is 1345 sec(-
CC 1) for the hydrolysis of pNP-hexanoate. kcat is 519 sec(-1) for the
CC hydrolysis of pNP-octanoate. kcat is 1531 sec(-1) for the hydrolysis
CC of pNP-dodecanoate. {ECO:0000269|PubMed:30502092};
CC pH dependence:
CC Optimum pH is 9 for PET film hydrolysis (PubMed:26965627). Optimum pH
CC is 9 for PET (commercial drinking bottle) hydrolysis. Optimum pH is
CC 6.5-8.0 for BHET hydrolysis (PubMed:29603535). Optimum pH is 8.0 for
CC the hydrolysis of pNP-esters. The enzyme is active at pH 6-10, has an
CC optimal pH range of 7-9 and it is rapidly inactivated below pH 7.0 or
CC above pH 9.0 (PubMed:30502092). {ECO:0000269|PubMed:26965627,
CC ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:30502092};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for PET film hydrolysis
CC (PubMed:26965627). Optimum temperature is 30 degrees Celsius for PET
CC (commercial drinking bottle) hydrolysis and BHET hydrolysis
CC (PubMed:29603535). Optimum temperature is 35-45 degrees Celsius for
CC the hydrolysis of pNP-esters. Remains active even at 65 degrees
CC Celsius (about 60% of maximum activity) (PubMed:30502092).
CC {ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:29603535,
CC ECO:0000269|PubMed:30502092};
CC -!- PATHWAY: Xenobiotic degradation. {ECO:0000305|PubMed:26965627}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29374183}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26965627}.
CC -!- INDUCTION: Highly up-regulated during growth on PET film.
CC {ECO:0000269|PubMed:26965627}.
CC -!- DOMAIN: PETase retains the ancestral alpha/beta-hydrolase fold but
CC exhibits a more open active-site cleft than homologous cutinases.
CC {ECO:0000269|PubMed:29666242}.
CC -!- BIOTECHNOLOGY: Has potential for application in environmental
CC remediation and biological recycling of PET and PEF waste products.
CC {ECO:0000305|PubMed:26965627, ECO:0000305|PubMed:29666242}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of plastic and men - Issue
CC 181 of July 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/181/";
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DR EMBL; BBYR01000074; GAP38373.1; -; Genomic_DNA.
DR RefSeq; WP_054022242.1; NZ_BBYR01000074.1.
DR PDB; 5XFY; X-ray; 1.40 A; A=30-290.
DR PDB; 5XFZ; X-ray; 1.55 A; A=30-290.
DR PDB; 5XG0; X-ray; 1.58 A; A/B/C=30-290.
DR PDB; 5XH2; X-ray; 1.20 A; A=30-290.
DR PDB; 5XH3; X-ray; 1.30 A; A=30-290.
DR PDB; 5XJH; X-ray; 1.54 A; A=34-290.
DR PDB; 5YFE; X-ray; 1.39 A; A=27-290.
DR PDB; 5YNS; X-ray; 1.36 A; A=34-290.
DR PDB; 6ANE; X-ray; 2.02 A; A/B/C=29-290.
DR PDB; 6EQD; X-ray; 1.70 A; A/B/C=1-290.
DR PDB; 6EQE; X-ray; 0.92 A; A=1-290.
DR PDB; 6EQF; X-ray; 1.70 A; A=1-290.
DR PDB; 6EQG; X-ray; 1.80 A; A/B/C=1-290.
DR PDB; 6EQH; X-ray; 1.58 A; A/B/C=1-290.
DR PDB; 6IJ3; X-ray; 1.40 A; A=34-290.
DR PDB; 6IJ4; X-ray; 1.86 A; A=34-290.
DR PDB; 6IJ5; X-ray; 1.72 A; A=34-290.
DR PDB; 6IJ6; X-ray; 1.95 A; A=34-290.
DR PDB; 6ILW; X-ray; 1.57 A; A=28-290.
DR PDB; 6ILX; X-ray; 1.45 A; A=28-290.
DR PDB; 6KUO; X-ray; 1.90 A; A=34-290.
DR PDB; 6KUQ; X-ray; 1.91 A; A=34-290.
DR PDB; 6KUS; X-ray; 1.80 A; A=34-290.
DR PDB; 6KY5; X-ray; 1.63 A; A/B=1-290.
DR PDB; 6QGC; X-ray; 2.00 A; A/B/C/D=1-290.
DR PDB; 7CQB; X-ray; 1.86 A; A=30-290.
DR PDB; 7CY0; X-ray; 1.32 A; A=30-290.
DR PDB; 7OSB; X-ray; 1.45 A; A/B/C=1-290.
DR PDB; 7SH6; X-ray; 1.44 A; A=27-290.
DR PDBsum; 5XFY; -.
DR PDBsum; 5XFZ; -.
DR PDBsum; 5XG0; -.
DR PDBsum; 5XH2; -.
DR PDBsum; 5XH3; -.
DR PDBsum; 5XJH; -.
DR PDBsum; 5YFE; -.
DR PDBsum; 5YNS; -.
DR PDBsum; 6ANE; -.
DR PDBsum; 6EQD; -.
DR PDBsum; 6EQE; -.
DR PDBsum; 6EQF; -.
DR PDBsum; 6EQG; -.
DR PDBsum; 6EQH; -.
DR PDBsum; 6IJ3; -.
DR PDBsum; 6IJ4; -.
DR PDBsum; 6IJ5; -.
DR PDBsum; 6IJ6; -.
DR PDBsum; 6ILW; -.
DR PDBsum; 6ILX; -.
DR PDBsum; 6KUO; -.
DR PDBsum; 6KUQ; -.
DR PDBsum; 6KUS; -.
DR PDBsum; 6KY5; -.
DR PDBsum; 6QGC; -.
DR PDBsum; 7CQB; -.
DR PDBsum; 7CY0; -.
DR PDBsum; 7OSB; -.
DR PDBsum; 7SH6; -.
DR AlphaFoldDB; A0A0K8P6T7; -.
DR SMR; A0A0K8P6T7; -.
DR ESTHER; idesa-peth; Polyesterase-lipase-cutinase.
DR EnsemblBacteria; GAP38373; GAP38373; ISF6_4831.
DR KEGG; ag:GAP38373; -.
DR OrthoDB; 685252at2; -.
DR BioCyc; MetaCyc:MON-19898; -.
DR BRENDA; 3.1.1.101; 14869.
DR SABIO-RK; A0A0K8P6T7; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002925; Dienelactn_hydro.
DR Pfam; PF01738; DLH; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Reference proteome; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..290
FT /note="Poly(ethylene terephthalate) hydrolase"
FT /id="PRO_5005513763"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29235460,
FT ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535,
FT ECO:0000305|PubMed:29666242"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:29235460,
FT ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535,
FT ECO:0000305|PubMed:29666242"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:29235460,
FT ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535,
FT ECO:0000305|PubMed:29666242"
FT BINDING 87
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000269|PubMed:29235460"
FT BINDING 161
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000269|PubMed:29235460"
FT BINDING 185
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000305|PubMed:29235460,
FT ECO:0000305|PubMed:29666242"
FT DISULFID 203..239
FT /evidence="ECO:0000269|PubMed:29235460,
FT ECO:0000269|PubMed:29374183, ECO:0000269|PubMed:29590588,
FT ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242,
FT ECO:0000269|PubMed:30502092, ECO:0000269|PubMed:30979881,
FT ECO:0000269|Ref.8, ECO:0007744|PDB:5XFY,
FT ECO:0007744|PDB:5XJH, ECO:0007744|PDB:5YFE,
FT ECO:0007744|PDB:6ANE, ECO:0007744|PDB:6EQD,
FT ECO:0007744|PDB:6IJ3, ECO:0007744|PDB:6ILW,
FT ECO:0007744|PDB:6QGC"
FT DISULFID 273..289
FT /evidence="ECO:0000269|PubMed:29235460,
FT ECO:0000269|PubMed:29374183, ECO:0000269|PubMed:29590588,
FT ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242,
FT ECO:0000269|PubMed:30502092, ECO:0000269|PubMed:30979881,
FT ECO:0000269|Ref.8, ECO:0007744|PDB:5XFY,
FT ECO:0007744|PDB:5XJH, ECO:0007744|PDB:5YFE,
FT ECO:0007744|PDB:6ANE, ECO:0007744|PDB:6EQD,
FT ECO:0007744|PDB:6IJ3, ECO:0007744|PDB:6ILW,
FT ECO:0007744|PDB:6QGC"
FT MUTAGEN 87
FT /note="Y->A: Displays increased enzymatic activity on PET
FT bottle. Displays decreased enzymatic activity on PET film
FT and on BHET."
FT /evidence="ECO:0000269|PubMed:29374183,
FT ECO:0000269|PubMed:29603535"
FT MUTAGEN 93
FT /note="S->M: Increases activity towards 1-naphthyl
FT butyrate."
FT /evidence="ECO:0000269|PubMed:30502092"
FT MUTAGEN 119
FT /note="Q->A: Displays decreased enzymatic activity on PET
FT bottle and on BHET."
FT /evidence="ECO:0000269|PubMed:29603535"
FT MUTAGEN 121
FT /note="S->E: Displays increased thermostability and
FT increased PET degradation activity by 14-fold at 40 degrees
FT Celsius; when associated with H-186 and A-280."
FT /evidence="ECO:0000269|Ref.8"
FT MUTAGEN 159
FT /note="W->A: Displays decreased enzymatic activity on PET
FT film and on BHET."
FT /evidence="ECO:0000269|PubMed:29374183"
FT MUTAGEN 159
FT /note="W->F: Increases activity towards 1-naphthyl
FT butyrate."
FT /evidence="ECO:0000269|PubMed:30502092"
FT MUTAGEN 159
FT /note="W->H: Displays increased enzymatic activity on PET
FT bottle and on BHET. Exhibits improved PET and PEF
FT degradation capacity relative to wild-type PETase; when
FT associated with F-238."
FT /evidence="ECO:0000269|PubMed:29603535,
FT ECO:0000269|PubMed:29666242"
FT MUTAGEN 160
FT /note="S->A: Loss of enzymatic activity on PET bottle and
FT on BHET."
FT /evidence="ECO:0000269|PubMed:29374183,
FT ECO:0000269|PubMed:29603535"
FT MUTAGEN 161
FT /note="M->A: Displays decreased enzymatic activity on PET
FT bottle and on BHET."
FT /evidence="ECO:0000269|PubMed:29603535"
FT MUTAGEN 185
FT /note="W->A: Exhibits highly impaired PET degradation
FT capacity relative to wild-type PETase. Also displays
FT decreased enzymatic activity on BHET."
FT /evidence="ECO:0000269|PubMed:29374183,
FT ECO:0000269|PubMed:29603535, ECO:0000269|PubMed:29666242"
FT MUTAGEN 186
FT /note="D->H: Displays increased thermostability and
FT increased PET degradation activity by 14-fold at 40 degrees
FT Celsius; when associated with E-121 and A-280."
FT /evidence="ECO:0000269|Ref.8"
FT MUTAGEN 203
FT /note="C->A: Displays decreased enzymatic activity on PET
FT film and on BHET; when associated with A-239."
FT /evidence="ECO:0000269|PubMed:29374183"
FT MUTAGEN 206
FT /note="D->A: Loss of enzymatic activity on PET bottle and
FT on BHET."
FT /evidence="ECO:0000269|PubMed:29374183,
FT ECO:0000269|PubMed:29603535"
FT MUTAGEN 214
FT /note="S->H: Displays increased enzymatic activity on PET
FT bottle."
FT /evidence="ECO:0000269|PubMed:29603535"
FT MUTAGEN 237
FT /note="H->A: Loss of enzymatic activity on PET bottle and
FT on BHET."
FT /evidence="ECO:0000269|PubMed:29374183,
FT ECO:0000269|PubMed:29603535"
FT MUTAGEN 238
FT /note="S->F: Displays decreased enzymatic activity on PET
FT film and on BHET. Exhibits improved PET and PEF degradation
FT capacity relative to wild-type PETase; when associated with
FT H-159."
FT /evidence="ECO:0000269|PubMed:29374183,
FT ECO:0000269|PubMed:29666242"
FT MUTAGEN 239
FT /note="C->A: Displays decreased enzymatic activity on PET
FT film and on BHET; when associated with A-203."
FT /evidence="ECO:0000269|PubMed:29374183"
FT MUTAGEN 241
FT /note="N->A: Displays decreased enzymatic activity on PET
FT film and on BHET."
FT /evidence="ECO:0000269|PubMed:29374183"
FT MUTAGEN 241
FT /note="N->F: Increases activity towards 1-naphthyl
FT butyrate."
FT /evidence="ECO:0000269|PubMed:30502092"
FT MUTAGEN 280
FT /note="R->A: Displays increased enzymatic activity on PET
FT film. Displays increased thermostability and increased PET
FT degradation activity by 14-fold at 40 degrees Celsius; when
FT associated with E-121 and H-186."
FT /evidence="ECO:0000269|PubMed:29374183, ECO:0000269|Ref.8"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6EQE"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:6EQE"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6IJ3"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6EQE"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6EQE"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6EQE"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:6EQE"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:6EQE"
SQ SEQUENCE 290 AA; 30247 MW; 8620A766B69749D2 CRC64;
MNFPRASRLM QAAVLGGLMA VSAAATAQTN PYARGPNPTA ASLEASAGPF TVRSFTVSRP
SGYGAGTVYY PTNAGGTVGA IAIVPGYTAR QSSIKWWGPR LASHGFVVIT IDTNSTLDQP
SSRSSQQMAA LRQVASLNGT SSSPIYGKVD TARMGVMGWS MGGGGSLISA ANNPSLKAAA
PQAPWDSSTN FSSVTVPTLI FACENDSIAP VNSSALPIYD SMSRNAKQFL EINGGSHSCA
NSGNSNQALI GKKGVAWMKR FMDNDTRYST FACENPNSTR VSDFRTANCS
