ID D1A646_THECD Unreviewed; 295 AA.
AC D1A646;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Poly(ethylene terephthalate) hydrolase {ECO:0000256|ARBA:ARBA00033780};
DE EC=3.1.1.101 {ECO:0000256|ARBA:ARBA00033764};
DE EC=3.1.1.74 {ECO:0000256|ARBA:ARBA00013095};
GN OrderedLocusNames=Tcur_4623 {ECO:0000313|EMBL:ACZ00145.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACZ00145.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACZ00145.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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:0000256|ARBA:ARBA00033707};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529;
CC Evidence={ECO:0000256|ARBA:ARBA00033707};
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:0000256|ARBA:ARBA00033629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000256|ARBA:ARBA00033629};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000256|ARBA:ARBA00034045};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001738; ACZ00145.1; -; Genomic_DNA.
DR RefSeq; WP_012854926.1; NC_013510.1.
DR AlphaFoldDB; D1A646; -.
DR SMR; D1A646; -.
DR STRING; 471852.Tcur_4623; -.
DR KEGG; tcu:Tcur_4623; -.
DR eggNOG; COG1073; Bacteria.
DR HOGENOM; CLU_052605_1_0_11; -.
DR OrthoDB; 1466228at2; -.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProt.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22946:SF9; POLYKETIDE TRANSFERASE AF380; 1.
DR PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:ACZ00145.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..295
FT /note="Poly(ethylene terephthalate) hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003019411"
SQ SEQUENCE 295 AA; 31868 MW; 9D294B7A20FF7A31 CRC64;
MKSRLRRSLR RLSVAAATVA AVGALTAVPA PAHAADNPYQ RGPDPTERSV TARRGPFAID
EISVNGGIGA GFNRGTIFYP TDRSQGTFGA VAVIPGFLSP ESLVRWFGPR LASQGFVVMT
LTTNGLTDTP ESRSEQLLAA LDYLTTRSQV RDRIDPSRLA VMGHSMGGGG SLAAAAKRPT
LRAAIPLAPW SLTKNWSDLT VPTLIIGAEN DNVAPVAGHS ERFYDSMTNV PEKAYLEMAG
GNHVDPTAES DLVAKFTISW LKRFVDDDTR YDQFLCPAPR PNRQISEYRD TCPHS
//
