PETH1_THEFU
ID PETH1_THEFU Reviewed; 319 AA.
AC G8GER6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Cutinase cut1 {ECO:0000303|PubMed:23604968};
DE EC=3.1.1.74 {ECO:0000305|PubMed:23604968};
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:32269349};
DE Flags: Precursor;
GN Name=cut_1 {ECO:0000303|PubMed:23604968};
OS Thermobifida fusca (Thermomonospora fusca).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=2021 {ECO:0000312|EMBL:AET05798.1};
RN [1] {ECO:0000312|EMBL:AET05798.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=NRRL B-8184 {ECO:0000303|PubMed:23604968};
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 [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RC STRAIN=DSM 43793 {ECO:0000303|PubMed:25545638}, and
RC 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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the
CC structure of plant cuticle (Probable). Shows esterase activity towards
CC p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters)
CC (PubMed:23604968, PubMed:25545638). Capable of degrading the plastic
CC poly(ethylene terephthalate) (PET), the most abundant polyester plastic
CC in the world (PubMed:25545638, PubMed:32269349).
CC {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638,
CC ECO:0000269|PubMed:32269349, 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};
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:23604968, ECO:0000269|PubMed:25545638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638};
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=(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:32269349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349};
CC -!- ACTIVITY REGULATION: Activated by magnesium ions (PubMed:25545638).
CC Activated by calcium ions (PubMed:25545638).
CC {ECO:0000269|PubMed:25545638}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=131 uM for pNP-butanoate (at 50 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:23604968};
CC Note=kcat is 178 sec(-1) for the hydrolysis of pNP-butanoate (at 50
CC degrees Celsius and pH 8). {ECO:0000269|PubMed:23604968};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:23604968};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius (PubMed:23604968). Optimum
CC temperature is 65 degrees Celsius (PubMed:32269349).
CC {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:32269349};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604968}. Periplasm
CC {ECO:0000269|PubMed:23604968}.
CC -!- BIOTECHNOLOGY: Shows promising applications in the laundry industry as
CC a cleansing agent, as it is thermostable and tolerant to surfactants
CC and organic solvents (PubMed:23604968). Has potential for application
CC in biological recycling of plastic waste products (PubMed:25545638,
CC PubMed:32269349). {ECO:0000269|PubMed:23604968,
CC ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; JN129499; AET05798.1; -; Genomic_DNA.
DR SMR; G8GER6; -.
DR ESTHER; thefu-q6a0i3; Polyesterase-lipase-cutinase.
DR OMA; ASHFFPQ; -.
DR BRENDA; 3.1.1.74; 6298.
DR SABIO-RK; G8GER6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; 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: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 Disulfide bond; Hydrolase; Periplasm; Secreted; Serine esterase; Signal.
FT SIGNAL 1..58
FT /evidence="ECO:0000255"
FT CHAIN 59..319
FT /note="Cutinase cut1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455609"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 118
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:F7IX06"
FT BINDING 189
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:F7IX06"
FT BINDING 213
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:F7IX06"
FT DISULFID 299..317
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
SQ SEQUENCE 319 AA; 34422 MW; A405BA67711B41BE CRC64;
MPPHAARPGP AQNRRGRAMA VITPRRERSS LLSRALRFTA AAATALVTAV SLAAPAHAAN
PYERGPNPTD ALLEARSGPF SVSEERASRF GADGFGGGTI YYPRENNTYG AVAISPGYTG
TQASVAWLGE RIASHGFVVI TIDTNTTLDQ PDSRARQLNA ALDYMINDAS SAVRSRIDSS
RLAVMGHSMG GGGTLRLASQ RPDLKAAIPL TPWHLNKNWS SVRVPTLIIG ADLDTIAPVL
THARPFYNSL PTSISKAYLE LDGATHFAPN IPNKIIGKYS VAWLKRFVDN DTRYTQFLCP
GPRDGLFGEV EEYRSTCPF
