ID COMT1_MEDSA Reviewed; 365 AA. AC P28002; D0VDZ3; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 22-FEB-2023, entry version 104. DE RecName: Full=Caffeic acid 3-O-methyltransferase {ECO:0000303|PubMed:1898010}; DE Short=CAOMT {ECO:0000305}; DE Short=COMT {ECO:0000303|PubMed:1898010}; DE EC=2.1.1.68 {ECO:0000269|PubMed:1898010}; DE AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase {ECO:0000305}; OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=cv. Apollo; RX PubMed=16668418; DOI=10.1104/pp.97.1.7; RA Gowri G., Bugos R.C., Campbell W.H., Maxwell C.A., Dixon R.A.; RT "Stress responses in alfalfa (Medicago sativa L). X. Molecular cloning and RT expression of S-adenosyl-L-methionine:caffeic acid 3-O-methyltransferase, a RT key enzyme of lignin biosynthesis."; RL Plant Physiol. 97:7-14(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RA Sullivan M.L., Xaypharath J.; RT "Sequence of a S-adenosyl-L-methionine: caffeic acid 3-0-methyltransferase RT cDNA from alfalfa leaves."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=1898010; DOI=10.1016/0003-9861(91)90492-2; RA Edwards R., Dixon R.A.; RT "Purification and characterization of S-adenosyl-L-methionine: caffeic acid RT 3-O-methyltransferase from suspension cultures of alfalfa (Medicago sativa RT L.)."; RL Arch. Biochem. Biophys. 287:372-379(1991). RN [4] {ECO:0007744|PDB:1KYW, ECO:0007744|PDB:1KYZ} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH RP S-ADENOSYL-L-HOMOCYSTEINE; FERULATE AND 5-HYDROXYFERULATE, AND SUBUNIT. RX PubMed=12084826; DOI=10.1105/tpc.001412; RA Zubieta C., Kota P., Ferrer J.-L., Dixon R.A., Noel J.P.; RT "Structural basis for the modulation of lignin monomer methylation by RT caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase."; RL Plant Cell 14:1265-1277(2002). CC -!- FUNCTION: Catalyzes the conversion of caffeic acid to ferulic acid and CC of 5-hydroxyferulic acid to sinapic acid (Probable) (PubMed:1898010). CC The resulting products may subsequently be converted to the CC corresponding alcohols that are incorporated into lignins (Probable) CC (PubMed:1898010). {ECO:0000269|PubMed:1898010, CC ECO:0000305|PubMed:16668418}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-caffeate + S-adenosyl-L-methionine = (E)-ferulate + H(+) + CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20225, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29749, ChEBI:CHEBI:57770, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789; EC=2.1.1.68; CC Evidence={ECO:0000269|PubMed:1898010}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20226; CC Evidence={ECO:0000269|PubMed:1898010}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-5-hydroxyferulate + S-adenosyl-L-methionine = (E)-sinapate CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60952, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30023, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:144381; CC Evidence={ECO:0000269|PubMed:1898010}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60953; CC Evidence={ECO:0000269|PubMed:1898010}; CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. CC {ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12084826}. CC -!- TISSUE SPECIFICITY: More abundant in roots and stems. CC {ECO:0000269|PubMed:16668418}. CC -!- INDUCTION: By infection, plant wounding, or elicitor treatment of cell CC cultures. {ECO:0000269|PubMed:16668418}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Cation-independent O-methyltransferase family. COMT CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M63853; AAB46623.1; -; mRNA. DR EMBL; GU066087; ACY06328.1; -; mRNA. DR PIR; T09673; T09673. DR PDB; 1KYW; X-ray; 2.40 A; A/C/F=1-365. DR PDB; 1KYZ; X-ray; 2.20 A; A/C/E=1-365. DR PDBsum; 1KYW; -. DR PDBsum; 1KYZ; -. DR AlphaFoldDB; P28002; -. DR SMR; P28002; -. DR BRENDA; 2.1.1.68; 3078. DR UniPathway; UPA00711; -. DR EvolutionaryTrace; P28002; -. DR GO; GO:0047763; F:caffeate 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:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB. 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; Lignin biosynthesis; Methyltransferase; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..365 FT /note="Caffeic acid 3-O-methyltransferase" FT /id="PRO_0000063204" FT ACT_SITE 269 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020, FT ECO:0000305|PubMed:12084826" FT ACT_SITE 297 FT /evidence="ECO:0000250|UniProtKB:F1DBB3" FT ACT_SITE 329 FT /evidence="ECO:0000250|UniProtKB:F1DBB3" FT BINDING 131 FT /ligand="(E)-ferulate" FT /ligand_id="ChEBI:CHEBI:29749" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 208 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 231 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 251 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 252 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 264 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 265 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYZ" FT BINDING 270 FT /ligand="(E)-5-hydroxyferulate" FT /ligand_id="ChEBI:CHEBI:144381" FT /evidence="ECO:0000269|PubMed:12084826, FT ECO:0007744|PDB:1KYW" FT CONFLICT 88 FT /note="I -> N (in Ref. 2; ACY06328)" FT /evidence="ECO:0000305" FT HELIX 16..27 FT /evidence="ECO:0007829|PDB:1KYZ" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 31..41 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 44..49 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 59..64 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 73..86 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 89..96 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 102..108 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 110..115 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 125..131 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 143..149 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 170..194 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:1KYZ" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:1KYW" FT HELIX 213..221 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:1KYZ" FT TURN 233..237 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:1KYZ" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 273..286 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:1KYZ" FT HELIX 308..323 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:1KYW" FT HELIX 332..342 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 347..353 FT /evidence="ECO:0007829|PDB:1KYZ" FT STRAND 356..361 FT /evidence="ECO:0007829|PDB:1KYZ" SQ SEQUENCE 365 AA; 39946 MW; C14B0D75F979C6B6 CRC64; MGSTGETQIT PTHISDEEAN LFAMQLASAS VLPMILKSAL ELDLLEIIAK AGPGAQISPI EIASQLPTTN PDAPVMLDRM LRLLACYIIL TCSVRTQQDG KVQRLYGLAT VAKYLVKNED GVSISALNLM NQDKVLMESW YHLKDAVLDG GIPFNKAYGM TAFEYHGTDP RFNKVFNKGM SDHSTITMKK ILETYTGFEG LKSLVDVGGG TGAVINTIVS KYPTIKGINF DLPHVIEDAP SYPGVEHVGG DMFVSIPKAD AVFMKWICHD WSDEHCLKFL KNCYEALPDN GKVIVAECIL PVAPDSSLAT KGVVHIDVIM LAHNPGGKER TQKEFEDLAK GAGFQGFKVH CNAFNTYIME FLKKV //