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Mono(2-hydroxyethyl) terephthalate hydrolase (MHET hydrolase) (MHETase) (EC 3.1.1.102)

 MHETH_IDESA             Reviewed;         603 AA.
A0A0K8P8E7;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
11-NOV-2015, sequence version 1.
28-FEB-2018, entry version 15.
RecName: Full=Mono(2-hydroxyethyl) terephthalate hydrolase {ECO:0000303|PubMed:26965627};
Short=MHET hydrolase {ECO:0000303|PubMed:26965627};
Short=MHETase {ECO:0000303|PubMed:26965627};
EC=3.1.1.102 {ECO:0000269|PubMed:26965627};
Flags: Precursor;
ORFNames=ISF6_0224 {ECO:0000312|EMBL:GAP38911.1};
Ideonella sakaiensis (strain 201-F6).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Ideonella.
NCBI_TaxID=1547922;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, INDUCTION BY PET, AND BIOTECHNOLOGY.
STRAIN=201-F6;
PubMed=26965627; DOI=10.1126/science.aad6359;
Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
Toyohara K., Miyamoto K., Kimura Y., Oda K.;
"A bacterium that degrades and assimilates poly(ethylene
terephthalate).";
Science 351:1196-1199(2016).
-!- FUNCTION: Involved in the degradation and assimilation of the
plastic poly(ethylene terephthalate) (PET), which allows
I.sakaiensis to use PET as its major energy and carbon source for
growth. Catalyzes the hydrolysis of mono(2-hydroxyethyl)
terephthalate into its two environmentally benign monomers,
terephthalate and ethylene glycol. Does not show activity against
PET, bis(hydroxyethyl) terephthalate (BHET), pNP-aliphatic esters
or typical aromatic ester compounds catalyzed by the tannase
family enzymes, such as ethyl gallate and ethyl ferulate.
{ECO:0000269|PubMed:26965627}.
-!- CATALYTIC ACTIVITY: Ethylene terephthalate + H(2)O = terephthalate
+ ethylene glycol. {ECO:0000269|PubMed:26965627}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.3 uM for mono(2-hydroxyethyl) terephthalate (at pH 7 and 30
degrees Celsius) {ECO:0000269|PubMed:26965627};
Note=kcat is 31 sec(-1) for the hydrolysis of mono(2-
hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius).
{ECO:0000269|PubMed:26965627};
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000305|PubMed:26965627}; Lipid-anchor {ECO:0000255|PROSITE-
ProRule:PRU00303, ECO:0000305|PubMed:26965627}.
-!- INDUCTION: Highly up-regulated during growth on PET film.
{ECO:0000269|PubMed:26965627}.
-!- BIOTECHNOLOGY: Has potential for application in environmental
remediation and biological recycling of PET waste products.
{ECO:0000305|PubMed:26965627}.
-!- MISCELLANEOUS: The calcium ion is located far from the active site
and appears to have a role in stabilization of the lid domain.
{ECO:0000250|UniProtKB:Q2UP89}.
-!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Of plastic and men
- Issue 181 of July 2016;
URL="https://web.expasy.org/spotlight/back_issues/181/";
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EMBL; BBYR01000104; GAP38911.1; -; Genomic_DNA.
EnsemblBacteria; GAP38911; GAP38911; ISF6_0224.
KEGG; ag:GAP38911; -.
KO; K21105; -.
BioCyc; MetaCyc:MONOMER-19899; -.
Proteomes; UP000037660; Unassembled WGS sequence.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071310; P:cellular response to organic substance; IDA:UniProtKB.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR011118; Tannase/feruloyl_esterase.
PANTHER; PTHR33938; PTHR33938; 1.
Pfam; PF07519; Tannase; 1.
SUPFAM; SSF53474; SSF53474; 3.
1: Evidence at protein level;
Cell outer membrane; Complete proteome; Disulfide bond; Hydrolase;
Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome;
Serine esterase; Signal.
SIGNAL 1 17 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 18 603 Mono(2-hydroxyethyl) terephthalate
hydrolase.
/FTId=PRO_5005513859.
COMPBIAS 25 44 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
ACT_SITE 225 225 Acyl-ester intermediate.
{ECO:0000250|UniProtKB:Q2UP89}.
ACT_SITE 492 492 Charge relay system.
{ECO:0000250|UniProtKB:Q2UP89}.
ACT_SITE 528 528 Charge relay system.
{ECO:0000250|UniProtKB:Q2UP89}.
METAL 304 304 Calcium. {ECO:0000250|UniProtKB:Q2UP89}.
METAL 307 307 Calcium. {ECO:0000250|UniProtKB:Q2UP89}.
METAL 309 309 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q2UP89}.
METAL 311 311 Calcium. {ECO:0000250|UniProtKB:Q2UP89}.
METAL 313 313 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q2UP89}.
LIPID 18 18 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
LIPID 18 18 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
DISULFID 224 529 {ECO:0000250|UniProtKB:Q2UP89}.
DISULFID 303 320 {ECO:0000250|UniProtKB:Q2UP89}.
DISULFID 577 599 {ECO:0000250|UniProtKB:Q2UP89}.
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


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