PETH2_THEFU
ID PETH2_THEFU Reviewed; 301 AA.
AC Q6A0I4; E0Z5H1; E5BBQ3; E9LVI0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Cutinase cut2 {ECO:0000303|PubMed:23604968};
DE Short=TfCut2 {ECO:0000303|PubMed:24728714};
DE EC=3.1.1.74 {ECO:0000305|PubMed:23604968, ECO:0000305|PubMed:24728714, ECO:0000305|PubMed:31690819, ECO:0000305|Ref.4};
DE AltName: Full=Acetylxylan esterase {ECO:0000303|PubMed:20816933};
DE AltName: Full=BTA-hydrolase 1 {ECO:0000303|PubMed:15638529};
DE AltName: Full=Poly(ethylene terephthalate) hydrolase {ECO:0000305};
DE Short=PET hydrolase {ECO:0000305};
DE Short=PETase {ECO:0000305};
DE EC=3.1.1.101 {ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:31690819, ECO:0000269|PubMed:32269349, ECO:0000269|Ref.4};
DE Flags: Precursor;
GN Name=cut2 {ECO:0000303|PubMed:23604968};
GN Synonyms=bta1 {ECO:0000303|PubMed:15638529}, cut1 {ECO:0000303|Ref.4},
GN TfH {ECO:0000303|PubMed:15638529};
OS Thermobifida fusca (Thermomonospora fusca).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=2021 {ECO:0000312|EMBL:CAH17553.1};
RN [1] {ECO:0000312|EMBL:CAH17553.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 43793 {ECO:0000303|PubMed:15638529};
RX PubMed=15638529; DOI=10.1021/bm049582t;
RA Kleeberg I., Welzel K., Vandenheuvel J., Mueller R.J., Deckwer W.D.;
RT "Characterization of a new extracellular hydrolase from Thermobifida fusca
RT degrading aliphatic-aromatic copolyesters.";
RL Biomacromolecules 6:262-270(2005).
RN [2] {ECO:0000312|EMBL:AET05799.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=NRRL B-8184 {ECO:0000312|EMBL:AET05799.1};
RX PubMed=23604968; DOI=10.1007/s12010-013-0219-x;
RA Hegde K., Veeranki V.D.;
RT "Production optimization and characterization of recombinant cutinases from
RT Thermobifida fusca sp. NRRL B-8184.";
RL Appl. Biochem. Biotechnol. 170:654-675(2013).
RN [3] {ECO:0000312|EMBL:ADM47605.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-301, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=NTU22 {ECO:0000312|EMBL:ADM47605.1};
RX PubMed=20816933; DOI=10.1016/j.bbrc.2010.08.136;
RA Huang Y.C., Chen G.H., Chen Y.F., Chen W.L., Yang C.H.;
RT "Heterologous expression of thermostable acetylxylan esterase gene from
RT Thermobifida fusca and its synergistic action with xylanase for the
RT production of xylooligosaccharides.";
RL Biochem. Biophys. Res. Commun. 400:718-723(2010).
RN [4] {ECO:0000312|EMBL:ADV92528.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-301, FUNCTION, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 44342 {ECO:0000303|Ref.4};
RX DOI=10.1021/ma200949p;
RA Herrero-Acero E., Ribitsch D., Steinkellner G., Gruber K., Greimel K.,
RA Eiteljoerg I., Trotscha E., Wei R., Zimmermann W., Zinn M.,
RA Cavaco-Paulo A., Freddi G., Schwab H., Guebitz G.;
RT "Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on
RT Kinetic Properties of Cutinases from Thermobifida.";
RL Macromolecules 44:4632-4640(2011).
RN [5] {ECO:0000312|EMBL:CBY05530.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-301.
RC STRAIN=DSM 6013 {ECO:0000303|Ref.5};
RA Wei R.;
RT "Cloning, expression and mutagenesis of cutinases isolated from
RT Thermobifida fusca KW3 and their applications for polyethylene
RT terephthalate hydrolysis.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ASP-214; ASP-244 AND GLU-293.
RC STRAIN=DSM 6013 {ECO:0000303|PubMed:25545638};
RX PubMed=25545638; DOI=10.1002/biot.201400620;
RA Then J., Wei R., Oeser T., Barth M., Belisario-Ferrari M.R., Schmidt J.,
RA Zimmermann W.;
RT "Ca2+ and Mg2+ binding site engineering increases the degradation of
RT polyethylene terephthalate films by polyester hydrolases from Thermobifida
RT fusca.";
RL Biotechnol. J. 10:592-598(2015).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLY-102; HIS-169 AND PHE-249.
RC STRAIN=DSM 6013 {ECO:0000303|PubMed:31690819};
RX PubMed=31690819; DOI=10.1038/s41598-019-52379-z;
RA Furukawa M., Kawakami N., Tomizawa A., Miyamoto K.;
RT "Efficient Degradation of Poly(ethylene terephthalate) with Thermobifida
RT fusca Cutinase Exhibiting Improved Catalytic Activity Generated using
RT Mutagenesis and Additive-based Approaches.";
RL Sci. Rep. 9:16038-16038(2019).
RN [8] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 43793 {ECO:0000303|PubMed:32269349};
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 [9] {ECO:0000305}
RP BIOTECHNOLOGY.
RX PubMed=33387709; DOI=10.1016/j.biortech.2020.124609;
RA Zhang Z., Wang W., Li D., Xiao J., Wu L., Geng X., Wu G., Zeng Z., Hu J.;
RT "Decolorization of molasses alcohol wastewater by thermophilic hydrolase
RT with practical application value.";
RL Bioresour. Technol. 323:124609-124609(2021).
RN [10] {ECO:0007744|PDB:4CG1, ECO:0007744|PDB:4CG2, ECO:0007744|PDB:4CG3}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 41-301, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP AND DISULFIDE BONDS.
RC STRAIN=DSM 6013 {ECO:0000303|PubMed:24728714};
RX PubMed=24728714; DOI=10.1007/s00253-014-5672-0;
RA Roth C., Wei R., Oeser T., Then J., Follner C., Zimmermann W., Strater N.;
RT "Structural and functional studies on a thermostable polyethylene
RT terephthalate degrading hydrolase from Thermobifida fusca.";
RL Appl. Microbiol. Biotechnol. 98:7815-7823(2014).
RN [11] {ECO:0007744|PDB:5ZOA}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 41-301.
RA Dong Q.L., Wu L., Wu J., Zhou J.H.;
RT "The crystal structure of a cutinase from Thermobifida fusca.";
RL Submitted (APR-2018) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the
CC structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714,
CC PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked
CC aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819,
CC PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638).
CC Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and
CC trilaurin, with a preference for short-chain substrates
CC (PubMed:15638529). Hydrolyzes the hemicellulose xylan
CC (PubMed:20816933). Capable of degrading the plastic poly(ethylene
CC terephthalate) (PET), the most abundant polyester plastic in the world
CC (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also
CC depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic
CC biodegradable polyester (PubMed:15638529). Hydrolyzes
CC polyoxyethylenesorbate esters with a preference for shorter chain
CC lengths (PubMed:20816933). {ECO:0000269|PubMed:15638529,
CC ECO:0000269|PubMed:20816933, ECO:0000269|PubMed:23604968,
CC ECO:0000269|PubMed:24728714, ECO:0000269|PubMed:25545638,
CC ECO:0000269|PubMed:31690819, ECO:0000269|PubMed:32269349,
CC ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pentanoate ester = an aliphatic alcohol + H(+) +
CC pentanoate; Xref=Rhea:RHEA:48436, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31011,
CC ChEBI:CHEBI:50871; Evidence={ECO:0000269|PubMed:23604968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48437;
CC Evidence={ECO:0000269|PubMed:23604968};
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:23604968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate +
CC H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658;
CC Evidence={ECO:0000269|PubMed:23604968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47361;
CC Evidence={ECO:0000269|PubMed:23604968};
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:23604968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365;
CC Evidence={ECO:0000269|PubMed:23604968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:23604968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389;
CC Evidence={ECO:0000269|PubMed:23604968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:23604968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393;
CC Evidence={ECO:0000269|PubMed:23604968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000305|PubMed:23604968};
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:23604968, ECO:0000269|PubMed:24728714,
CC ECO:0000269|Ref.4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:24728714,
CC ECO:0000269|Ref.4};
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:25545638, ECO:0000269|PubMed:31690819,
CC ECO:0000269|PubMed:32269349, ECO:0000269|Ref.4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:31690819,
CC ECO:0000269|PubMed:32269349, ECO:0000269|Ref.4};
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:15638529, ECO:0000269|PubMed:23604968,
CC ECO:0000269|PubMed:24728714, ECO:0000269|PubMed:25545638,
CC ECO:0000269|PubMed:31690819, ECO:0000269|Ref.4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:15638529, ECO:0000269|PubMed:23604968,
CC ECO:0000269|PubMed:24728714, ECO:0000269|PubMed:25545638,
CC ECO:0000269|PubMed:31690819, ECO:0000269|Ref.4};
CC -!- ACTIVITY REGULATION: Activated by magnesium ions (PubMed:25545638).
CC Activated by calcium ions (PubMed:25545638). Inhibited by the serine
CC hydrolase inhibitor phenylmethanesulfonyl fluoride (PMSF) (Probable).
CC {ECO:0000269|PubMed:25545638, ECO:0000305|PubMed:24728714}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=167 uM for pNP-acetate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.4};
CC KM=89 uM for pNP-butanoate (at 50 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:23604968};
CC KM=2100 uM for pNP-butanoate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.4};
CC Note=kcat is 39.5 sec(-1) with pNP-acetate as substrate (at 25
CC degrees Celsius and pH 7) (Ref.4). kcat is 253 sec(-1) with pNP-
CC butanoate as substrate (at 50 degrees Celsius and pH 8)
CC (PubMed:23604968). kcat is 30.9 sec(-1) with pNP-butanoate as
CC substrate (at 25 degrees Celsius and pH 7) (Ref.4).
CC {ECO:0000269|PubMed:23604968, ECO:0000269|Ref.4};
CC pH dependence:
CC Optimum pH is 8 (PubMed:23604968). Optimum pH is 6.0-6.5
CC (PubMed:15638529). Optimum pH is 7.5 (PubMed:20816933).
CC {ECO:0000269|PubMed:15638529, ECO:0000269|PubMed:20816933,
CC ECO:0000269|PubMed:23604968};
CC Temperature dependence:
CC Optimum temperature is 25-50 degrees Celsius (PubMed:24728714).
CC Optimum temperature is 55 degrees Celsius (PubMed:23604968). Optimum
CC temperature is 60 degrees Celsius (PubMed:20816933). Optimum
CC temperature is 65 degrees Celsius (PubMed:15638529, PubMed:31690819,
CC PubMed:32269349). {ECO:0000269|PubMed:15638529,
CC ECO:0000269|PubMed:20816933, ECO:0000269|PubMed:23604968,
CC ECO:0000269|PubMed:24728714, ECO:0000269|PubMed:31690819,
CC ECO:0000269|PubMed:32269349};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20816933}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604968}. Periplasm
CC {ECO:0000269|PubMed:23604968}.
CC -!- BIOTECHNOLOGY: Has potential for application in biological recycling of
CC plastic waste products (Ref.4, PubMed:25545638, PubMed:31690819,
CC PubMed:32269349). Shows promising applications in the laundry industry
CC as a cleansing agent, as it is thermostable and tolerant to surfactants
CC and organic solvents (PubMed:23604968). Also shows promising
CC applications in ethyl alcohol distillery processes as it may be
CC utilized for treatment of molasses wastewater (PubMed:33387709).
CC {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638,
CC ECO:0000269|PubMed:31690819, ECO:0000269|PubMed:32269349,
CC ECO:0000269|PubMed:33387709, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AJ810119; CAH17553.1; -; Genomic_DNA.
DR EMBL; JN129500; AET05799.1; -; Genomic_DNA.
DR EMBL; HM193859; ADM47605.1; -; Genomic_DNA.
DR EMBL; HQ147787; ADV92528.1; -; Genomic_DNA.
DR EMBL; FR727681; CBY05530.1; -; Genomic_DNA.
DR PDB; 4CG1; X-ray; 1.40 A; A=41-301.
DR PDB; 4CG2; X-ray; 1.44 A; A=41-301.
DR PDB; 4CG3; X-ray; 1.55 A; A=41-301.
DR PDB; 5ZOA; X-ray; 1.54 A; A=41-301.
DR PDBsum; 4CG1; -.
DR PDBsum; 4CG2; -.
DR PDBsum; 4CG3; -.
DR PDBsum; 5ZOA; -.
DR SMR; Q6A0I4; -.
DR ESTHER; thefu-q6a0i4; Polyesterase-lipase-cutinase.
DR OMA; ATHFTPN; -.
DR BRENDA; 3.1.1.101; 6298.
DR BRENDA; 3.1.1.102; 6298.
DR BRENDA; 3.1.1.74; 6298.
DR SABIO-RK; Q6A0I4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; 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; IPR041127; Chlorophyllase2.
DR Pfam; PF12740; Chlorophyllase2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Periplasm; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..301
FT /note="Cutinase cut2"
FT /evidence="ECO:0000255"
FT /id="PRO_5007707721"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24728714,
FT ECO:0007744|PDB:4CG2"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 100
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7,
FT ECO:0000305|PubMed:24728714"
FT BINDING 171
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7,
FT ECO:0000305|PubMed:24728714"
FT BINDING 195
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT DISULFID 281..299
FT /evidence="ECO:0000269|PubMed:24728714,
FT ECO:0007744|PDB:4CG1, ECO:0007744|PDB:4CG2,
FT ECO:0007744|PDB:4CG3"
FT MUTAGEN 102
FT /note="G->A: Increases activity on poly(ethylene
FT terephthalate) (PET)."
FT /evidence="ECO:0000269|PubMed:31690819"
FT MUTAGEN 169
FT /note="H->A: Decreases activity on poly(ethylene
FT terephthalate) (PET)."
FT /evidence="ECO:0000269|PubMed:31690819"
FT MUTAGEN 169
FT /note="H->W: Increases activity on poly(ethylene
FT terephthalate) (PET)."
FT /evidence="ECO:0000269|PubMed:31690819"
FT MUTAGEN 214
FT /note="D->R: Increases the thermal stability of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:25545638"
FT MUTAGEN 244
FT /note="D->R: Increases the thermal stability of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:25545638"
FT MUTAGEN 249
FT /note="F->S,A,V: Increases activity on poly(ethylene
FT terephthalate) (PET)."
FT /evidence="ECO:0000269|PubMed:31690819"
FT MUTAGEN 293
FT /note="E->R: Increases the thermal stability of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:25545638"
FT CONFLICT 40
FT /note="A -> M (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="S -> R (in Ref. 3; ADM47605, 4; ADV92528 and 5;
FT CBY05530)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="N -> S (in Ref. 3; ADM47605)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="T -> S (in Ref. 4; ADV92528 and 5; CBY05530)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="T -> R (in Ref. 4; ADV92528)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..226
FT /note="ATHAK -> LTHAR (in Ref. 4; ADV92528)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="S -> T (in Ref. 4; ADV92528)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="R -> W (in Ref. 3; ADM47605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 32218 MW; 4FF805EBE36D888F CRC64;
MAVMTPRRER SSLLSRALQV TAAAATALVT AVSLAAPAHA ANPYERGPNP TDALLEASSG
PFSVSEENVS RLSASGFGGG TIYYPRENNT YGAVAISPGY TGTEASIAWL GERIASHGFV
VITIDTITTL DQPDSRAEQL NAALNHMINR ASSTVRSRID SSRLAVMGHS MGGGGTLRLA
SQRPDLKAAI PLTPWHLNKN WSSVTVPTLI IGADLDTIAP VATHAKPFYN SLPSSISKAY
LELDGATHFA PNIPNKIIGK YSVAWLKRFV DNDTRYTQFL CPGPRDGLFG EVEEYRSTCP
F
