MOMT_CATRO
ID MOMT_CATRO Reviewed; 348 AA.
AC Q8GSN1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Myricetin O-methyltransferase;
DE EC=2.1.1.267;
DE AltName: Full=CrOMT2 {ECO:0000303|PubMed:12482447};
DE AltName: Full=Flavonoid O-methyltransferase {ECO:0000312|EMBL:AAM97497.1};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM97497.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 119-130; 142-151;
RP 170-194; 290-297 AND 334-341, FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT
RP MET-1, AND MASS SPECTROMETRY.
RX PubMed=12482447; DOI=10.1016/s0031-9422(02)00483-1;
RA Cacace S., Schroder G., Wehinger E., Strack D., Schmidt J., Schroder J.;
RT "A flavonol O-methyltransferase from Catharanthus roseus performing two
RT sequential methylations.";
RL Phytochemistry 62:127-137(2003).
CC -!- FUNCTION: Methylates myricetin and dihydromyricetin at 2 sites.
CC Inactive towards 16-hydroxytabersonine, the phenylpropanoids 5-
CC hydroxyferulate, caffeate and their CoA-esters, flavones and flavanones
CC possessing 2 or 3 B-ring hydroxyl groups.
CC {ECO:0000269|PubMed:12482447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-
CC L-homocysteine + a 3'-methoxyflavonoid.; EC=2.1.1.267;
CC Evidence={ECO:0000269|PubMed:12482447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid =
CC S-adenosyl-L-homocysteine + a 3',5'-dimethoxyflavonoid.;
CC EC=2.1.1.267; Evidence={ECO:0000269|PubMed:12482447};
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12482447}.
CC -!- MASS SPECTROMETRY: Mass=39191; Mass_error=3; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:12482447};
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}.
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DR EMBL; AY127568; AAM97497.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GSN1; -.
DR SMR; Q8GSN1; -.
DR iPTMnet; Q8GSN1; -.
DR KEGG; ag:AAM97497; -.
DR BioCyc; MetaCyc:MON-12684; -.
DR BRENDA; 2.1.1.267; 1211.
DR GO; GO:0070448; F:laricitrin 5'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033799; F:myricetin 3'-O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization 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; 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 Acetylation; Direct protein sequencing; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..348
FT /note="Myricetin O-methyltransferase"
FT /id="PRO_0000405018"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O24529,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O24529,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O24529,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O24529,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O24529,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O24529,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12482447"
SQ SEQUENCE 348 AA; 39145 MW; 95AB7CD672372493 CRC64;
MELQSSEIRN AQAHFFTQVF SFTSMSSLKC AVQLGIPDAI HSHGKPMALS DLTNSLPINP
SKAPYIYRLM RILVAAGYFS EEEKNVYSLT PFTRLLLKND PLNSISMVLG VNQIAELKAW
NAMSEWFQNE DLTAFETAHG KNFWDFGAED KYGKNFDGVM AADSILVSKM LIPEFNYLFE
GLDSLVDVGG GTGTIAKAIA KSFPDLKCTV FDLPHVVANL ESTENLEFVG GDMFEKIPSA
NAILLKWILH DWKDEECVKV LKMCRKAIPE KEKGGKVILI ETVLMDSKKH ENEEAVKAQI
SSDIDMMVFF TAKERTEEEW ATLFREAGFS GYKIFPMIDF RSPIEVYP
