COMT1_MEDSA
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 03-AUG-2022, entry version 101.
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]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND
RP 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}.
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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 PRIDE; 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 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; 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 REGION 162..180
FT /note="Substrate binding"
FT /evidence="ECO:0000305"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000305|PubMed:12084826, ECO:0007744|PDB:1KYW"
FT ACT_SITE 297
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 329
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 130..136
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12084826,
FT ECO:0007744|PDB:1KYZ"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12084826,
FT ECO:0007744|PDB:1KYZ"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000269|PubMed:12084826, ECO:0007744|PDB:1KYW,
FT ECO:0007744|PDB:1KYZ"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12084826,
FT ECO:0007744|PDB:1KYW, ECO:0007744|PDB:1KYZ"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12084826,
FT ECO:0007744|PDB:1KYW, ECO:0007744|PDB:1KYZ"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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
