PETH1_THEFY
ID PETH1_THEFY Reviewed; 319 AA.
AC Q47RJ7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cutinase;
DE EC=3.1.1.74 {ECO:0000269|PubMed:18658138};
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};
DE Flags: Precursor;
GN OrderedLocusNames=Tfu_0882 {ECO:0000312|EMBL:AAZ54920.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the
CC structure of plant cuticle (PubMed:18658138). Shows esterase activity
CC towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters)
CC (PubMed:18658138, PubMed:25545638). Also hydrolyzes the triglyceride
CC triolein (PubMed:18658138). Capable of degrading the plastic
CC poly(ethylene terephthalate) (PET), the most abundant polyester plastic
CC in the world (PubMed:25545638). {ECO:0000269|PubMed:18658138,
CC ECO:0000269|PubMed:25545638}.
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:18658138, ECO:0000269|PubMed:25545638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:25545638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000269|PubMed:18658138};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000269|PubMed:25545638};
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)
CC (PubMed:18658138). {ECO:0000269|PubMed:18658138,
CC ECO:0000269|PubMed:25545638}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:18658138};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:18658138};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}.
CC Periplasm {ECO:0000250|UniProtKB:G8GER6}.
CC -!- BIOTECHNOLOGY: Has potential for application in biological recycling of
CC plastic waste products. {ECO:0000269|PubMed:25545638}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; CP000088; AAZ54920.1; -; Genomic_DNA.
DR SMR; Q47RJ7; -.
DR STRING; 269800.Tfu_0882; -.
DR ESTHER; thefu-q6a0i3; Polyesterase-lipase-cutinase.
DR EnsemblBacteria; AAZ54920; AAZ54920; Tfu_0882.
DR KEGG; tfu:Tfu_0882; -.
DR eggNOG; COG4188; Bacteria.
DR HOGENOM; CLU_052605_1_0_11; -.
DR OMA; ASHFFPQ; -.
DR BRENDA; 3.1.1.3; 6298.
DR SABIO-RK; Q47RJ7; -.
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 GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
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..40
FT /evidence="ECO:0000305|PubMed:18658138"
FT CHAIN 41..319
FT /note="Cutinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455610"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18658138"
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:A0A0K8P6T7"
FT BINDING 189
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 213
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
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
