PETH1_THECS
ID PETH1_THECS Reviewed; 262 AA.
AC E9LVH8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Cutinase 1 {ECO:0000303|Ref.1};
DE EC=3.1.1.74 {ECO:0000305|PubMed:23592055, ECO:0000305|PubMed:23718548, ECO:0000305|PubMed:28671263, ECO:0000305|Ref.1};
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:23592055, ECO:0000269|PubMed:23718548, ECO:0000269|Ref.1, ECO:0000305|PubMed:28671263};
DE Flags: Fragment;
GN Name=cut1 {ECO:0000303|Ref.1};
OS Thermobifida cellulosilytica.
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=144786;
RN [1] {ECO:0000312|EMBL:ADV92526.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
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 [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RX PubMed=23718548; DOI=10.1021/bm400140u;
RA Ribitsch D., Yebra A.O., Zitzenbacher S., Wu J., Nowitsch S.,
RA Steinkellner G., Greimel K., Doliska A., Oberdorfer G., Gruber C.C.,
RA Gruber K., Schwab H., Stana-Kleinschek K., Acero E.H., Guebitz G.M.;
RT "Fusion of binding domains to Thermobifida cellulosilytica cutinase to tune
RT sorption characteristics and enhancing PET hydrolysis.";
RL Biomacromolecules 14:1769-1776(2013).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RX PubMed=23592055; DOI=10.1002/bit.24930;
RA Herrero Acero E., Ribitsch D., Dellacher A., Zitzenbacher S., Marold A.,
RA Steinkellner G., Gruber K., Schwab H., Guebitz G.M.;
RT "Surface engineering of a cutinase from Thermobifida cellulosilytica for
RT improved polyester hydrolysis.";
RL Biotechnol. Bioeng. 110:2581-2590(2013).
RN [4] {ECO:0007744|PDB:5LUI}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP DISULFIDE BONDS, AND BIOTECHNOLOGY.
RX PubMed=28671263; DOI=10.1002/bit.26372;
RA Ribitsch D., Hromic A., Zitzenbacher S., Zartl B., Gamerith C., Pellis A.,
RA Jungbauer A., Lyskowski A., Steinkellner G., Gruber K., Tscheliessnig R.,
RA Acero E.H., Guebitz G.M.;
RT "Small cause, large effect: Structural characterization of cutinases from
RT Thermobifida cellulosilytica.";
RL Biotechnol. Bioeng. 114:2481-2488(2017).
CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the
CC structure of plant cuticle (Ref.1). Shows esterase activity towards p-
CC nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1,
CC PubMed:23718548, PubMed:23592055). Capable of degrading the plastic
CC poly(ethylene terephthalate) (PET), the most abundant polyester plastic
CC in the world (Ref.1, PubMed:23718548, PubMed:23592055). Capable of
CC degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263).
CC {ECO:0000269|PubMed:23592055, ECO:0000269|PubMed:23718548,
CC ECO:0000269|PubMed:28671263, ECO:0000269|Ref.1}.
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:23592055, ECO:0000269|Ref.1,
CC ECO:0000305|PubMed:28671263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1};
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:23592055, ECO:0000269|PubMed:23718548,
CC ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|PubMed:23718548,
CC ECO:0000269|Ref.1};
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:23592055, ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000305|PubMed:23592055, ECO:0000305|PubMed:28671263,
CC ECO:0000305|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=127 uM for pNP-acetate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.1};
CC KM=1.5 mM for pNP-acetate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:23592055};
CC KM=1483 uM for pNP-butanoate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|Ref.1};
CC KM=800 uM for pNP-butanoate {ECO:0000269|PubMed:23718548};
CC KM=800 uM for pNP-butanoate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:23592055};
CC Note=kcat is 211.9 sec(-1) with pNP-acetate as substrate (at 25
CC degrees Celsius and pH 7) (Ref.1). kcat is 436 sec(-1) with pNP-
CC acetate as substrate (at 25 degrees Celsius and pH 7)
CC (PubMed:23592055). kcat is 195.1 sec(-1) with pNP-butanoate as
CC substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 325 sec(-
CC 1) with pNP-butanoate as substrate (PubMed:23718548). kcat is 327
CC sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH
CC 7) (Ref.1). {ECO:0000269|PubMed:23592055,
CC ECO:0000269|PubMed:23718548, ECO:0000269|Ref.1};
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:23592055,
CC ECO:0000269|PubMed:23718548, ECO:0000269|PubMed:28671263,
CC ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; HQ147785; ADV92526.1; -; Genomic_DNA.
DR PDB; 5LUI; X-ray; 1.50 A; A=1-262.
DR PDBsum; 5LUI; -.
DR SMR; E9LVH8; -.
DR ESTHER; thefu-q6a0i4; Polyesterase-lipase-cutinase.
DR BRENDA; 3.1.1.101; 12709.
DR BRENDA; 3.1.1.74; 12709.
DR SABIO-RK; E9LVH8; -.
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 3D-structure; Disulfide bond; Hydrolase; Periplasm; Secreted;
KW Serine esterase.
FT CHAIN <1..262
FT /note="Cutinase 1"
FT /id="PRO_0000455611"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 61
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 132
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT BINDING 156
FT /ligand="poly(ethylene terephthalate)"
FT /ligand_id="ChEBI:CHEBI:131701"
FT /evidence="ECO:0000250|UniProtKB:A0A0K8P6T7"
FT DISULFID 242..260
FT /evidence="ECO:0000269|PubMed:28671263,
FT ECO:0007744|PDB:5LUI"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ADV92526.1"
SQ SEQUENCE 262 AA; 28306 MW; 2B0D14F07ABA40A8 CRC64;
MANPYERGPN PTDALLEASS GPFSVSEENV SRLSASGFGG GTIYYPRENN TYGAVAISPG
YTGTEASIAW LGERIASHGF VVITIDTITT LDQPDSRAEQ LNAALNHMIN RASSTVRSRI
DSSRLAVMGH SMGGGGTLRL ASQRPDLKAA IPLTPWHLNK NWSSVTVPTL IIGADLDTIA
PVATHAKPFY NSLPSSISKA YLELDGATHF APNIPNKIIG KYSVAWLKRF VDNDTRYTQF
LCPGPRDGLF GEVEEYRSTC PF
