CMT1_TRILO
ID CMT1_TRILO Reviewed; 467 AA.
AC D3H5H5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Chlorophenol O-methyltransferase {ECO:0000303|PubMed:12957890};
DE Short=COMPT {ECO:0000303|PubMed:12957890};
DE EC=2.1.1.136 {ECO:0000269|PubMed:20144725};
GN Name=cmt1 {ECO:0000303|PubMed:20144725};
OS Trichoderma longibrachiatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RC STRAIN=CECT 20431;
RX PubMed=20144725; DOI=10.1016/j.fgb.2010.02.002;
RA Feltrer R., Alvarez-Rodriguez M.L., Barreiro C., Godio R.P., Coque J.J.;
RT "Characterization of a novel 2,4,6-trichlorophenol-inducible gene encoding
RT chlorophenol O-methyltransferase from Trichoderma longibrachiatum
RT responsible for the formation of chloroanisoles and detoxification of
RT chlorophenols.";
RL Fungal Genet. Biol. 47:458-467(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND INDUCTION.
RX PubMed=12957890; DOI=10.1128/aem.69.9.5089-5095.2003;
RA Coque J.J., Alvarez-Rodriguez M.L., Larriba G.;
RT "Characterization of an inducible chlorophenol O-methyltransferase from
RT Trichoderma longibrachiatum involved in the formation of chloroanisoles and
RT determination of its role in cork taint of wines.";
RL Appl. Environ. Microbiol. 69:5089-5095(2003).
RN [3]
RP REVIEW ON BIOTECHNOLOGY.
RX PubMed=28842039; DOI=10.1016/j.talanta.2017.07.029;
RA Tarasov A., Rauhut D., Jung R.;
RT "'Cork taint' responsible compounds. Determination of haloanisoles and
RT halophenols in cork matrix: A review.";
RL Talanta 175:82-92(2017).
CC -!- FUNCTION: Chlorophenol O-methyltransferase that methylates
CC chlorophenols into chloroanisoles which are thought to be responsible
CC for cork taint of wines (PubMed:20144725, PubMed:12957890). The only
CC single chlorophenol (CP) methylated is 2-CP; neither 3-CP nor 4-CP are
CC effective substrates (PubMed:12957890). Within the dichlorophenols
CC (DCPs), 2,4-DCP supports the highest rate of O-methylation, and the
CC activity decreases in the following order: 2,3-DCP, 2,5-DCP, 2,6-DCP,
CC and 3,4-DCP (PubMed:12957890). Within the trichlorophenol (TCP) group,
CC the maximal activity is observed with 2,3,4-TCP, whereas there is
CC increasingly reduced activity with 2,4,5-TCP, 2,4,6-TCP, and 2,3,6-TCP
CC (PubMed:12957890). The only tetrachlorophenol (TeCP) that is methylated
CC is 2,3,4,5-TeCP, since no activity can be detected with 2,3,4,6-TeCP
CC and 2,3,5,6-TeCP (PubMed:12957890). Is also able to methylate other
CC halogenated phenols containing fluoro or bromo substituents, whereas
CC other hydroxylated compounds, such as hydroxylated benzoic acids,
CC hydroxybenzaldehydes, phenol, 2-metoxyphenol, and dihydroxybenzene,
CC were not methylated (PubMed:12957890). {ECO:0000269|PubMed:12957890,
CC ECO:0000269|PubMed:20144725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,4,6-trichlorophenol + S-adenosyl-L-methionine = 2,4,6-
CC trichloroanisole + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:18909,
CC ChEBI:CHEBI:19333, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:140426; EC=2.1.1.136;
CC Evidence={ECO:0000269|PubMed:12957890};
CC -!- ACTIVITY REGULATION: S-adenosyl-L-homocysteine acts as a competitive
CC inhibitor (PubMed:12957890). Also strongly inhibited by low
CC concentrations of several metal ions, such as Cu(2+), Hg(2+), Zn(2+),
CC and Ag(+), and to a lesser extent by p-chloromercuribenzoic acid, but
CC it is not significantly affected by several thiols or other thiol
CC reagents (PubMed:12957890). {ECO:0000269|PubMed:12957890}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=136 uM for 2,4,6-trichlorophenol (2,4,6-TCP)
CC {ECO:0000269|PubMed:12957890};
CC KM=284 uM for S-adenosyl-L-methionine (SAM)
CC {ECO:0000269|PubMed:12957890};
CC pH dependence:
CC Optimum pH is 8.2-8.5. {ECO:0000269|PubMed:12957890};
CC Temperature dependence:
CC Optimum temperature is 28 degrees Celsius.
CC {ECO:0000269|PubMed:12957890};
CC -!- INDUCTION: Expression is specifically induced by several chlorophenols,
CC especially if they contained three or more chlorine atoms in their
CC structures, such as 2,4,6-trichlorophenol (PubMed:20144725,
CC PubMed:12957890). {ECO:0000269|PubMed:12957890,
CC ECO:0000269|PubMed:20144725}.
CC -!- BIOTECHNOLOGY: Chloroanisoles such as 2,4,6-trichloroanisole (TCA) are
CC known compounds which are usually associated with wine faults
CC (PubMed:28842039). They belong to the family of haloanisoles which are
CC key substances responsible for cork taint in wines (PubMed:28842039).
CC {ECO:0000303|PubMed:28842039}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Tainted - Issue 204 of June
CC 2018;
CC URL="https://web.expasy.org/spotlight/back_issues/204/";
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DR EMBL; FN554867; CBG37723.1; -; Genomic_DNA.
DR AlphaFoldDB; D3H5H5; -.
DR SMR; D3H5H5; -.
DR GO; GO:0030790; F:chlorophenol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..467
FT /note="Chlorophenol O-methyltransferase"
FT /id="PRO_0000444106"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 467 AA; 52461 MW; E23B1F53AA97E414 CRC64;
MAELRAPSSL STERNGSASN TDVDKQKLNH LYQNGNKKTG SAESRMLVLA ETIRAETQKL
HAYLESNGIA QPDLSVDAPD DFPPLPDEIQ ESRQKIFLAS RELTDIVRGP RETVRYAVWS
YLDTLSLQLI NSYGIAKLVP LDAPIKLTEL QSKTPLEPVH LARALRHAMT NNIFREPSPG
YIAHTSSSRI LAQDPALQAW VGFNSEDAFP AAGHVLQALK DHPEAISSTH AGFNYAFNTV
GQEPMFATLG KDLARAKRFA QAMHSFSHGE GYKVSYFVDN YDLSEVDKRG GTFVDIGGSH
GFVSVELAKR WKDMKFIVED LPKTIESAPQ PISDDKTVAD RISLQAHDFF QEQPVKGADV
YFFRWIIHNH AKPYAVSILR NLIPALKPGA RVVINDYCIR EAGSENAWDE KLLRNMDMIM
GALLNAQERE EWEFRELFEA ADPRFKFKGV QRVENCKMSV IEAVWDE
