COMTS_PEUPR
ID COMTS_PEUPR Reviewed; 364 AA.
AC A0A4P8DY91;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Esculetin O-methyltransferase {ECO:0000303|PubMed:30934718};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|PubMed:30934718};
DE AltName: Full=Bergaptol O-methyltransferase {ECO:0000303|PubMed:30934718};
DE EC=2.1.1.69 {ECO:0000269|PubMed:30934718};
DE AltName: Full=Isoscopoletin O-methyltransferase {ECO:0000303|PubMed:30934718};
DE EC=2.1.1.- {ECO:0000269|PubMed:30934718};
DE AltName: Full=Scopoletin O-methyltransferase {ECO:0000303|PubMed:30934718};
DE EC=2.1.1.- {ECO:0000269|PubMed:30934718};
DE AltName: Full=Xanthotoxol O-methyltransferase {ECO:0000303|PubMed:30934718};
DE EC=2.1.1.70 {ECO:0000269|PubMed:30934718};
GN Name=COMT-S {ECO:0000303|PubMed:30934718};
OS Peucedanum praeruptorum (Kitagawia praeruptora).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Selineae; Peucedanum.
OX NCBI_TaxID=312531;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS), NUCLEOTIDE SEQUENCE [MRNA],
RP FUNCTION, MUTAGENESIS OF ASN-132; LEU-137; PHE-164; PRO-171; MET-181;
RP SER-185; ASP-232; LEU-233; ASP-252; MET-253; LYS-266; TRP-267; HIS-270;
RP ASP-271; ILE-317; ILE-320; MET-321 AND ASN-325, CATALYTIC ACTIVITY,
RP PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY UV AND HYDROGEN PEROXYDE.
RC TISSUE=Root;
RX PubMed=30934718; DOI=10.3390/ijms20071533;
RA Zhao Y., Wang N., Sui Z., Huang C., Zeng Z., Kong L.;
RT "The molecular and structural basis of O-methylation reaction in coumarin
RT biosynthesis in Peucedanum praeruptorum Dunn.";
RL Int. J. Mol. Sci. 20:0-0(2019).
CC -!- FUNCTION: O-methyltransferase involved in the biosynthesis of
CC methoxylated coumarins natural products such as isoscopoletin,
CC scopoletin, xanthotoxin and bergapten, photosensitizers used for
CC medical purpose such as treating psoriasis and vitiligo or facilitating
CC resistance to microbial infection and other stresses (PubMed:30934718).
CC Catalyzes the methylation of esculetin, bergaptol and xanthotoxol, but
CC seems inactive on scopoletin and isoscopoletin (PubMed:30934718).
CC {ECO:0000269|PubMed:30934718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-
CC L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69;
CC Evidence={ECO:0000269|PubMed:30934718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809;
CC Evidence={ECO:0000269|PubMed:30934718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + xanthotoxol = H(+) + S-adenosyl-L-
CC homocysteine + xanthotoxin; Xref=Rhea:RHEA:17901, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15709, ChEBI:CHEBI:18358, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.70;
CC Evidence={ECO:0000269|PubMed:30934718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17902;
CC Evidence={ECO:0000269|PubMed:30934718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=esculetin + S-adenosyl-L-methionine = H(+) + isoscopoletin +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68944, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81484,
CC ChEBI:CHEBI:490095; Evidence={ECO:0000269|PubMed:30934718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68945;
CC Evidence={ECO:0000269|PubMed:30934718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=esculetin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-
CC homocysteine + scopoletin; Xref=Rhea:RHEA:68948, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17488, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:490095; Evidence={ECO:0000269|PubMed:30934718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68949;
CC Evidence={ECO:0000269|PubMed:30934718};
CC -!- ACTIVITY REGULATION: Inhibited by zinc Zn(2+), copper Cu(2+) and silver
CC Ag(+) ions. {ECO:0000269|PubMed:30934718}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:30934718};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:30934718}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30934718}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28002}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:30934718}.
CC -!- INDUCTION: Induced by UV light and hydrogen peroxyde H(2)O(2).
CC {ECO:0000269|PubMed:30934718}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000305}.
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DR EMBL; MK005887; QCO31674.1; -; mRNA.
DR PDB; 6IWT; X-ray; 2.53 A; A/B=1-364.
DR PDBsum; 6IWT; -.
DR SMR; A0A4P8DY91; -.
DR GO; GO:0016206; F:catechol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102084; F:L-dopa O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102938; F:orcinol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009805; P:coumarin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEP:UniProtKB.
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; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 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 3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..364
FT /note="Esculetin O-methyltransferase"
FT /id="PRO_0000454880"
FT REGION 163..181
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 131..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT SITE 132
FT /note="Determines the catalytic selectivity of hydroxyl
FT groups in esculetin between the 6-hydroxyl and 7-hydroxyl
FT groups"
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 132
FT /note="N->A: Modified catalytic selectivity of hydroxyl
FT groups in esculetin with an enhanced production of
FT scopoletin, acquired possibility to use scopoletin and
FT isoscopoletin as substrates, but abolished synthesis of
FT isoscopoletin."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 137
FT /note="L->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 164
FT /note="F->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 171
FT /note="P->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 181
FT /note="M->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 185
FT /note="S->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 232
FT /note="D->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 233
FT /note="L->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 252
FT /note="D->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 253
FT /note="M->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 266
FT /note="K->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 267
FT /note="W->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 270
FT /note="H->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 271
FT /note="D->A: Reduced activity, but acquired possibility to
FT use scopoletin and isoscopoletin as substrates and
FT increased efficiency on bergaptol."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 317
FT /note="I->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 320
FT /note="I->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 321
FT /note="M->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:30934718"
FT MUTAGEN 325
FT /note="N->A: Reduced activity, but acquired possibility to
FT use scopoletin and isoscopoletin as substrates and
FT increased efficiency on bergaptol and xanthotoxol."
FT /evidence="ECO:0000269|PubMed:30934718"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:6IWT"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 171..195
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6IWT"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:6IWT"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 309..324
FT /evidence="ECO:0007829|PDB:6IWT"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:6IWT"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:6IWT"
SQ SEQUENCE 364 AA; 39979 MW; 0BF63C6792825736 CRC64;
MTTTELIPPT IQVDEEEEEA CMFAMQLASA SVLPMVLKSA IELDLLESIA KAGPGAYVSP
SELAAKLPSS QPDTPVMLDR ILRLLASYSV LKCKVQDLPQ GGVERLYALA PVCKFLTKNS
DGVSMAPLLL MNQDKILMES WYHLKDAVLD GGIPFNKAYG MTAFEYHGKD PRFNKVFNLG
MSNHSTITMK KILQTYNGFA GLKTVVDVGG GTGATLNMII SKYPNIKGIN FDLPHVVEDA
PSYPGVEHVG GDMFVSVPEG DAIFMKWICH DWSDAHCLSF LKNCYKALPQ NGKVILAECI
LPEAPDSKLT TKNVIHIDVI MLAHNPGGKE RTEKEFEALG KMAGFKSFNK VCCAHNTWIM
EFLK
