PETH1_THEAE
ID PETH1_THEAE Reviewed; 296 AA.
AC D4Q9N1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Cutinase est1 {ECO:0000303|PubMed:20393707};
DE EC=3.1.1.74 {ECO:0000305};
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:25910960};
DE Flags: Precursor;
GN Name=est1 {ECO:0000303|PubMed:20393707};
OS Thermobifida alba (Thermomonospora alba).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=53522;
RN [1] {ECO:0000312|EMBL:BAI99230.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20393707; DOI=10.1007/s00253-010-2555-x;
RA Hu X., Thumarat U., Zhang X., Tang M., Kawai F.;
RT "Diversity of polyester-degrading bacteria in compost and molecular
RT analysis of a thermoactive esterase from Thermobifida alba AHK119.";
RL Appl. Microbiol. Biotechnol. 87:771-779(2010).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP BIOTECHNOLOGY, AND MUTAGENESIS OF ALA-64 AND THR-249.
RX PubMed=25910960; DOI=10.1016/j.jbiosc.2015.03.006;
RA Thumarat U., Kawabata T., Nakajima M., Nakajima H., Sugiyama A., Yazaki K.,
RA Tada T., Waku T., Tanaka N., Kawai F.;
RT "Comparison of genetic structures and biochemical properties of tandem
RT cutinase-type polyesterases from Thermobifida alba AHK119.";
RL J. Biosci. Bioeng. 120:491-497(2015).
CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the
CC structure of plant cuticle (PubMed:25910960). Shows esterase activity
CC towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters)
CC (PubMed:25910960). Capable of degrading the plastic poly(ethylene
CC terephthalate) (PET), the most abundant polyester plastic in the world
CC (PubMed:25910960). Can also depolymerize the synthetic polyester
CC poly(epsilon-caprolactone) (PCL) (PubMed:25910960).
CC {ECO:0000269|PubMed:25910960}.
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:0000305|PubMed:25910960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000305|PubMed:25910960};
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:25910960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:25910960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000305|PubMed:25910960};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:25910960};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:25910960};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:F7IX06}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}.
CC Periplasm {ECO:0000250|UniProtKB:G8GER6}.
CC -!- INDUCTION: Expression is not induced by the synthetic polyester
CC poly(butylene succinate-co-adipate) (PBSA).
CC {ECO:0000269|PubMed:25910960}.
CC -!- BIOTECHNOLOGY: Has potential for application in biological recycling of
CC plastic waste products. {ECO:0000269|PubMed:25910960}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AB445476; BAI99230.2; -; Genomic_DNA.
DR SMR; D4Q9N1; -.
DR ESTHER; 9acto-d4q9n1; Polyesterase-lipase-cutinase.
DR BRENDA; 3.1.1.74; 6312.
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; IEA:UniProtKB-KW.
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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..296
FT /note="Cutinase est1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003062113"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 95
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 166
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 190
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT DISULFID 276..294
FT /evidence="ECO:0000250|UniProtKB:F7IX06"
FT MUTAGEN 64
FT /note="A->V: Increases thermostability and activity on pNP-
FT butyrate; when associated with P-249."
FT /evidence="ECO:0000269|PubMed:25910960"
FT MUTAGEN 249
FT /note="T->P: Increases thermostability and activity on pNP-
FT butyrate; when associated with V-64."
FT /evidence="ECO:0000269|PubMed:25910960"
SQ SEQUENCE 296 AA; 31787 MW; 997F11B4DDDF086F CRC64;
MSVTTPRREA SLLSRAVAVA AAAAATVALA APAQAANPYE RGPNPTESML EARSGPFSVS
EERASRLGAD GFGGGTIYYP RENNTYGAIA ISPGYTGTQS SIAWLGERIA SHGFVVIAID
TNTTLDQPDS RARQLNAALD YMLTDASSSV RNRIDASRLA VMGHSMGGGG TLRLASQRPD
LKAAIPLTPW HLNKSWRDIT VPTLIIGADL DTIAPVSSHS EPFYNSIPSS TDKAYLELNN
ATHFAPNITN KTIGMYSVAW LKRFVDEDTR YTQFLCPGPR TGLLSDVDEY RSTCPF
