ID   Q9ZTU2_LOLPR            Unreviewed;       360 AA.
AC   Q9ZTU2;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Caffeic acid O-methyltransferase {ECO:0000313|EMBL:AAD10253.1};
DE            EC=2.1.1.6 {ECO:0000313|EMBL:AAD10253.1};
GN   Name=OMT1 {ECO:0000313|EMBL:AAD10253.1};
OS   Lolium perenne (Perennial ryegrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type);
OC   Loliodinae; Loliinae; Lolium.
OX   NCBI_TaxID=4522 {ECO:0000313|EMBL:AAD10253.1};
RN   [1] {ECO:0000313|EMBL:AAD10253.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Heath R.L., Huxley H., Stone B.A., Spangenberg G.;
RT   "cDNA cloning and differential expression of three caffeic acid O-
RT   methyltransferase homologues from Lolium perenne.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3P9C, ECO:0007829|PDB:3P9I}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE.
RX   PubMed=21177481; DOI=10.1105/tpc.110.077578;
RA   Louie G.V., Bowman M.E., Tu Y., Mouradov A., Spangenberg G., Noel J.P.;
RT   "Structure-function analyses of a caffeic acid O-methyltransferase from
RT   perennial ryegrass reveal the molecular basis for substrate preference.";
RL   Plant Cell 22:4114-4127(2010).
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DR   EMBL; AF033538; AAD10253.1; -; mRNA.
DR   PDB; 3P9C; X-ray; 1.80 A; A=1-360.
DR   PDB; 3P9I; X-ray; 1.85 A; A/B/C/D=1-360.
DR   PDB; 3P9K; X-ray; 2.25 A; A/B/C/D=1-360.
DR   PDBsum; 3P9C; -.
DR   PDBsum; 3P9I; -.
DR   PDBsum; 3P9K; -.
DR   AlphaFoldDB; Q9ZTU2; -.
DR   SMR; Q9ZTU2; -.
DR   EvolutionaryTrace; Q9ZTU2; -.
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:0102938; F:orcinol O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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:SF199; FLAVONE 3'-O-METHYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR11746; O-METHYLTRANSFERASE; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3P9C, ECO:0007829|PDB:3P9I};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AAD10253.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000313|EMBL:AAD10253.1}.
FT   DOMAIN          31..82
FT                   /note="Plant methyltransferase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08100"
FT   DOMAIN          137..341
FT                   /note="O-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00891"
FT   ACT_SITE        266
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005739-1"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0007829|PDB:3P9I, ECO:0007829|PDB:3P9K"
FT   BINDING         228
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0007829|PDB:3P9C, ECO:0007829|PDB:3P9I"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0007829|PDB:3P9C, ECO:0007829|PDB:3P9I"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0007829|PDB:3P9C, ECO:0007829|PDB:3P9I"
FT   BINDING         262
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0007829|PDB:3P9C, ECO:0007829|PDB:3P9I"
SQ   SEQUENCE   360 AA;  38769 MW;  B018C8300962FA14 CRC64;
     MGSTAADMAA SADEDACMFA LQLASSSVLP MTLKNAIELG LLEILVAAGG KSLTPTEVAA
     KLPSAANPEA PDMVDRILRL LASYNVVTCL VEEGKDGRLS RSYGAAPVCK FLTPNEDGVS
     MAALALMNQD KVLMESWYYL KDAVLDGGIP FNKAYGMSAF EYHGTDPRFN RVFNEGMKNH
     SIIITKKLLE LYHGFEGLGT LVDVGGGVGA TVAAIAAHYP TIKGVNFDLP HVISEAPQFP
     GVTHVGGDMF KEVPSGDTIL MKWILHDWSD QHCATLLKNC YDALPAHGKV VLVQCILPVN
     PEANPSSQGV FHVDMIMLAH NPGGRERYER EFQALARGAG FTGVKSTYIY ANAWAIEFTK
//