ID   OMT1_SECCE              Reviewed;         355 AA.
AC   Q84XW5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Daphnetin O-methyltransferase 1 {ECO:0000303|PubMed:12480941};
DE            Short=ScOMT1 {ECO:0000303|PubMed:12480941};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|PubMed:12480941};
GN   Name=OMT1 {ECO:0000303|PubMed:12480941};
OS   Secale cereale (Rye).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX   NCBI_TaxID=4550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP   INDUCTION BY COLD AND PHOTOSYSTEM II EXCITATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=cv. Musketeer;
RX   PubMed=12480941; DOI=10.1074/jbc.m209439200;
RA   N'Dong C., Anzellotti D., Ibrahim R.K., Huner N.P.A., Sarhan F.;
RT   "Daphnetin methylation by a novel O-methyltransferase is associated with
RT   cold acclimation and photosystem II excitation pressure in rye.";
RL   J. Biol. Chem. 278:6854-6861(2003).
CC   -!- FUNCTION: O-methyltransferase involved in the biosynthesis of coumarins
CC       natural products such as daphnetin derivatives (PubMed:12480941).
CC       Catalyzes specifically the methylation of daphnetin (7,8-
CC       dihydroxycoumarin) to produce hydrangetin (7-hydroxy-8-methoxycoumarin)
CC       (PubMed:12480941). Probably involved in acclimation to low temperature
CC       conditions (PubMed:12480941). {ECO:0000269|PubMed:12480941}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroxycoumarin + S-adenosyl-L-methionine = 7-hydroxy-8-
CC         methoxycoumarin + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:68960, ChEBI:CHEBI:15378, ChEBI:CHEBI:17313,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:180544;
CC         Evidence={ECO:0000269|PubMed:12480941};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68961;
CC         Evidence={ECO:0000269|PubMed:12480941};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=152 uM for 7,8-dihydroxycoumarin {ECO:0000269|PubMed:12480941};
CC         KM=19 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12480941};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:12480941}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:12480941}.
CC   -!- INDUCTION: Induced by cold and photosystem II excitation pressure by
CC       high light illumination. {ECO:0000269|PubMed:12480941}.
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; AY177404; AAO23335.1; -; mRNA.
DR   GO; GO:0102358; F:daphnetin-8-O-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IDA: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   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..355
FT                   /note="Daphnetin O-methyltransferase 1"
FT                   /id="PRO_0000454879"
FT   ACT_SITE        260
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         222
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002"
SQ   SEQUENCE   355 AA;  38845 MW;  FE5ACBDB58A86989 CRC64;
     MPSSQAQADL WRHTLYYLTS MGLRCAVKLG IPTAIHNLGG VSSLPDLAAA LSIPASKQPF
     LGRLMRALVT SGVFANGKER LLGGLFRLNP LSRILVEGVV AEEHHSQTSF VLAGTSRHYM
     EAALGMADWF KKDATGPVPT VFEDVHSASL FDESTAALDP ELDALVTEGL AAHDNLGIGT
     IIREFHDLFK GLVSLTDFCC GDGTTSRAIT KAHPHVKFTV LDLPKVIDKT PSDGIVNYFA
     GDLFHTVPKA QAVMLKLVLH HLSYEDCFKI LTQCKDAIPS REEGGKVIVI DIVVAPSLGQ
     VMFKEQTLMD ILMLVFTRGR QRSENNWHEL FTKAGFSDYK IVKKLGARGV IEVYK