CAMT_MEDSA
ID CAMT_MEDSA Reviewed; 247 AA.
AC Q40313;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Caffeoyl-CoA O-methyltransferase;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase;
DE Short=CCoAMT;
DE Short=CCoAOMT;
GN Name=CCOMT;
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].
RC STRAIN=cv. Apollo;
RX PubMed=9662519; DOI=10.1104/pp.117.3.761;
RA Inoue K., Sewalt V.J.H., Ballance G.M., Ni W., Sturzer C., Dixon R.A.;
RT "Developmental expression and substrate specificities of alfalfa caffeic
RT acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase in
RT relation to lignification.";
RL Plant Physiol. 117:761-770(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND COFACTOR.
RX PubMed=15734921; DOI=10.1104/pp.104.048751;
RA Ferrer J.-L., Zubieta C., Dixon R.A., Noel J.P.;
RT "Crystal structures of alfalfa caffeoyl coenzyme A 3-O-methyltransferase.";
RL Plant Physiol. 137:1009-1017(2005).
CC -!- FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-
CC hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of
CC feruloylated polysaccharides. Involved in the reinforcement of the
CC plant cell wall. Also involved in the responding to wounding or
CC pathogen challenge by the increased formation of cell wall-bound
CC ferulic acid polymers.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15734921};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15734921};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15734921};
CC Note=Binds 1 divalent metal cation per subunit. Fully active with
CC Ca(2+), Mg(2+) or Zn(2+) ions. Active at 35% with Mn(2+) ion.
CC {ECO:0000269|PubMed:15734921};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15734921}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; U20736; AAC28973.1; -; mRNA.
DR PIR; T09399; T09399.
DR PDB; 1SUI; X-ray; 2.70 A; A/B/C/D=1-247.
DR PDB; 1SUS; X-ray; 2.70 A; A/B/C/D=1-247.
DR PDBsum; 1SUI; -.
DR PDBsum; 1SUS; -.
DR AlphaFoldDB; Q40313; -.
DR SMR; Q40313; -.
DR BRENDA; 2.1.1.104; 3078.
DR UniPathway; UPA00711; -.
DR EvolutionaryTrace; Q40313; -.
DR GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Lignin biosynthesis; Metal-binding;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..247
FT /note="Caffeoyl-CoA O-methyltransferase"
FT /id="PRO_0000165686"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15734921"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 87..88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15734921"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 190
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15734921"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15734921"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1SUI"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1SUS"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1SUI"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1SUI"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1SUI"
SQ SEQUENCE 247 AA; 27999 MW; 2B82576EB21E3DA8 CRC64;
MATNEDQKQT ESGRHQEVGH KSLLQSDALY QYILETSVFP REHEAMKELR EVTAKHPWNI
MTTSADEGQF LSMLLKLINA KNTMEIGVYT GYSLLATALA IPEDGKILAM DINKENYELG
LPVIKKAGVD HKIDFREGPA LPVLDEMIKD EKNHGSYDFI FVDADKDNYL NYHKRLIDLV
KVGGVIGYDN TLWNGSVVAP PDAPLRKYVR YYRDFVLELN KALAVDPRIE ICMLPVGDGI
TICRRIK
