MHETH_IDESA
ID MHETH_IDESA Reviewed; 603 AA.
AC A0A0K8P8E7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Mono(2-hydroxyethyl) terephthalate hydrolase {ECO:0000303|PubMed:26965627};
DE Short=MHET hydrolase {ECO:0000303|PubMed:26965627};
DE Short=MHETase {ECO:0000303|PubMed:26965627};
DE EC=3.1.1.102 {ECO:0000269|PubMed:26965627};
DE Flags: Precursor;
GN ORFNames=ISF6_0224 {ECO:0000312|EMBL:GAP38911.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Ideonella.
OX NCBI_TaxID=1547922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, INDUCTION BY PET, AND BIOTECHNOLOGY.
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6;
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEXES WITH CALCIUM; SUBSTRATE
RP ANALOG 4-(2-HYDROXYETHYLCARBAMOYL)BENZOATE AND BENZOATE, CATALYTIC
RP ACTIVITY, ACTIVE SITE, DISULFIDE BONDS, AND MUTAGENESIS OF SER-225;
RP ARG-411; SER-416; PHE-424; ASP-492 AND HIS-528.
RX PubMed=30979881; DOI=10.1038/s41467-019-09326-3;
RA Palm G.J., Reisky L., Bottcher D., Muller H., Michels E.A.P., Walczak M.C.,
RA Berndt L., Weiss M.S., Bornscheuer U.T., Weber G.;
RT "Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a
RT substrate.";
RL Nat. Commun. 10:1717-1717(2019).
CC -!- FUNCTION: Involved in the degradation and assimilation of the plastic
CC poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use
CC PET as its major energy and carbon source for growth. Likely acts
CC synergistically with PETase to depolymerize PET. Catalyzes the
CC hydrolysis of mono(2-hydroxyethyl) terephthalate (MHET) into its two
CC environmentally benign monomers, terephthalate and ethylene glycol.
CC Does not show activity against PET, bis(hydroxyethyl) terephthalate
CC (BHET), pNP-aliphatic esters or typical aromatic ester compounds
CC catalyzed by the tannase family enzymes, such as ethyl gallate and
CC ethyl ferulate. {ECO:0000269|PubMed:26965627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = ethylene glycol
CC + H(+) + terephthalate; Xref=Rhea:RHEA:49532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30043, ChEBI:CHEBI:30742,
CC ChEBI:CHEBI:131704; EC=3.1.1.102;
CC Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30979881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49533;
CC Evidence={ECO:0000269|PubMed:26965627};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.3 uM for mono(2-hydroxyethyl) terephthalate (at pH 7 and 30
CC degrees Celsius) {ECO:0000269|PubMed:26965627};
CC Note=kcat is 31 sec(-1) for the hydrolysis of mono(2-hydroxyethyl)
CC terephthalate (at pH 7 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:26965627};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:26965627}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000305|PubMed:26965627}.
CC -!- INDUCTION: Highly up-regulated during growth on PET film.
CC {ECO:0000269|PubMed:26965627}.
CC -!- BIOTECHNOLOGY: Has potential for application in environmental
CC remediation and biological recycling of PET waste products.
CC {ECO:0000305|PubMed:26965627}.
CC -!- MISCELLANEOUS: The calcium ion is located far from the active site and
CC appears to have a role in stabilization of the lid domain.
CC {ECO:0000250|UniProtKB:Q2UP89}.
CC -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of plastic and men - Issue
CC 181 of July 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/181/";
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DR EMBL; BBYR01000104; GAP38911.1; -; Genomic_DNA.
DR RefSeq; WP_054022745.1; NZ_BBYR01000104.1.
DR PDB; 6JTT; X-ray; 2.51 A; A/B/C=17-603.
DR PDB; 6JTU; X-ray; 2.10 A; A/B/C=17-603.
DR PDB; 6QG9; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=20-603.
DR PDB; 6QGA; X-ray; 2.10 A; A/B/C/D/E/F=20-603.
DR PDB; 6QGB; X-ray; 2.20 A; A/B/C/D/E/F=20-603.
DR PDB; 6QZ1; X-ray; 1.70 A; A=40-603.
DR PDB; 6QZ2; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-603.
DR PDB; 6QZ3; X-ray; 1.60 A; A=1-603.
DR PDB; 6QZ4; X-ray; 1.80 A; A/B=1-603.
DR PDBsum; 6JTT; -.
DR PDBsum; 6JTU; -.
DR PDBsum; 6QG9; -.
DR PDBsum; 6QGA; -.
DR PDBsum; 6QGB; -.
DR PDBsum; 6QZ1; -.
DR PDBsum; 6QZ2; -.
DR PDBsum; 6QZ3; -.
DR PDBsum; 6QZ4; -.
DR AlphaFoldDB; A0A0K8P8E7; -.
DR SMR; A0A0K8P8E7; -.
DR STRING; 1547922.ISF6_0224; -.
DR ESTHER; idesa-mheth; Tannase.
DR EnsemblBacteria; GAP38911; GAP38911; ISF6_0224.
DR KEGG; ag:GAP38911; -.
DR OMA; AATDMGH; -.
DR BioCyc; MetaCyc:MON-19899; -.
DR BRENDA; 3.1.1.102; 14869.
DR SABIO-RK; A0A0K8P8E7; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011118; Tannase/feruloyl_esterase.
DR PANTHER; PTHR33938; PTHR33938; 1.
DR Pfam; PF07519; Tannase; 1.
DR SUPFAM; SSF53474; SSF53474; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell outer membrane; Disulfide bond; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..603
FT /note="Mono(2-hydroxyethyl) terephthalate hydrolase"
FT /id="PRO_5005513859"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|PubMed:30979881"
FT ACT_SITE 492
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:30979881"
FT ACT_SITE 528
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:30979881"
FT BINDING 132
FT /ligand="4-[(2-hydroxyethoxy)carbonyl]benzoate"
FT /ligand_id="ChEBI:CHEBI:131704"
FT /evidence="ECO:0000305|PubMed:30979881"
FT BINDING 226
FT /ligand="4-[(2-hydroxyethoxy)carbonyl]benzoate"
FT /ligand_id="ChEBI:CHEBI:131704"
FT /evidence="ECO:0000305|PubMed:30979881"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30979881"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30979881"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30979881"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30979881"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30979881"
FT BINDING 411
FT /ligand="4-[(2-hydroxyethoxy)carbonyl]benzoate"
FT /ligand_id="ChEBI:CHEBI:131704"
FT /evidence="ECO:0000305|PubMed:30979881"
FT BINDING 416
FT /ligand="4-[(2-hydroxyethoxy)carbonyl]benzoate"
FT /ligand_id="ChEBI:CHEBI:131704"
FT /evidence="ECO:0000305|PubMed:30979881"
FT BINDING 528
FT /ligand="4-[(2-hydroxyethoxy)carbonyl]benzoate"
FT /ligand_id="ChEBI:CHEBI:131704"
FT /evidence="ECO:0000305|PubMed:30979881"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 51..92
FT /evidence="ECO:0000269|PubMed:30979881"
FT DISULFID 224..529
FT /evidence="ECO:0000269|PubMed:30979881"
FT DISULFID 303..320
FT /evidence="ECO:0000269|PubMed:30979881"
FT DISULFID 340..348
FT /evidence="ECO:0000269|PubMed:30979881"
FT DISULFID 577..599
FT /evidence="ECO:0000269|PubMed:30979881"
FT MUTAGEN 225
FT /note="S->A: Loss of catalytic activity towards MHET."
FT /evidence="ECO:0000269|PubMed:30979881"
FT MUTAGEN 411
FT /note="R->A,Q: Almost complete loss of catalytic activity
FT towards MHET."
FT /evidence="ECO:0000269|PubMed:30979881"
FT MUTAGEN 416
FT /note="S->A: Gains a low activity towards BHET (bis-(2-
FT hydroxyethyl) terephthalate); when associated with N-424."
FT /evidence="ECO:0000269|PubMed:30979881"
FT MUTAGEN 424
FT /note="F->N: Gains a low activity towards BHET (bis-(2-
FT hydroxyethyl) terephthalate); when associated with A-416."
FT /evidence="ECO:0000269|PubMed:30979881"
FT MUTAGEN 492
FT /note="D->A: Loss of catalytic activity towards MHET."
FT /evidence="ECO:0000269|PubMed:30979881"
FT MUTAGEN 528
FT /note="H->A: Loss of catalytic activity towards MHET."
FT /evidence="ECO:0000269|PubMed:30979881"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6QZ4"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 90..102
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 108..120
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6QG9"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 410..413
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:6QZ3"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 497..510
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 541..550
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:6QZ3"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:6QZ3"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:6QZ3"
SQ SEQUENCE 603 AA; 63103 MW; E9317BE82796A187 CRC64;
MQTTVTTMLL ASVALAACAG GGSTPLPLPQ QQPPQQEPPP PPVPLASRAA CEALKDGNGD
MVWPNAATVV EVAAWRDAAP ATASAAALPE HCEVSGAIAK RTGIDGYPYE IKFRLRMPAE
WNGRFFMEGG SGTNGSLSAA TGSIGGGQIA SALSRNFATI ATDGGHDNAV NDNPDALGTV
AFGLDPQARL DMGYNSYDQV TQAGKAAVAR FYGRAADKSY FIGCSEGGRE GMMLSQRFPS
HYDGIVAGAP GYQLPKAGIS GAWTTQSLAP AAVGLDAQGV PLINKSFSDA DLHLLSQAIL
GTCDALDGLA DGIVDNYRAC QAAFDPATAA NPANGQALQC VGAKTADCLS PVQVTAIKRA
MAGPVNSAGT PLYNRWAWDA GMSGLSGTTY NQGWRSWWLG SFNSSANNAQ RVSGFSARSW
LVDFATPPEP MPMTQVAARM MKFDFDIDPL KIWATSGQFT QSSMDWHGAT STDLAAFRDR
GGKMILYHGM SDAAFSALDT ADYYERLGAA MPGAAGFARL FLVPGMNHCS GGPGTDRFDM
LTPLVAWVER GEAPDQISAW SGTPGYFGVA ARTRPLCPYP QIARYKGSGD INTEANFACA
APP
