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Protein

Caffeoyl-CoA O-methyltransferase

Gene

CCOMT

Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.

Catalytic activityi

S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA.

Cofactori

Ca2+1 Publication, Mg2+1 Publication, Zn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Fully active with Ca2+, Mg2+ or Zn2+ ions. Active at 35% with Mn2+ ion.1 Publication

Pathwayi: phenylpropanoid biosynthesis

This protein is involved in the pathway phenylpropanoid biosynthesis, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenylpropanoid biosynthesis and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei21Substrate; via amide nitrogen1 Publication1
Binding sitei63S-adenosyl-L-methionine; via amide nitrogen1 Publication1
Binding sitei85S-adenosyl-L-methionine1 Publication1
Binding sitei93S-adenosyl-L-methionine1 Publication1
Binding sitei111S-adenosyl-L-methionine1 Publication1
Binding sitei140S-adenosyl-L-methionine; via amide nitrogen1 Publication1
Metal bindingi163Divalent metal cation1 Publication1
Binding sitei163Substrate1 Publication1
Binding sitei165S-adenosyl-L-methionine1 Publication1
Metal bindingi189Divalent metal cation1 Publication1
Metal bindingi190Divalent metal cation1 Publication1
Binding sitei194Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lignin biosynthesis

Keywords - Ligandi

Calcium, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.104. 3078.
UniPathwayiUPA00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Caffeoyl-CoA O-methyltransferase (EC:2.1.1.104)
Alternative name(s):
Trans-caffeoyl-CoA 3-O-methyltransferase
Short name:
CCoAMT
Short name:
CCoAOMT
Gene namesi
Name:CCOMT
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001656861 – 247Caffeoyl-CoA O-methyltransferaseAdd BLAST247

Proteomic databases

PRIDEiQ40313.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 25Combined sources3
Helixi27 – 37Combined sources11
Beta strandi39 – 41Combined sources3
Helixi45 – 54Combined sources10
Helixi59 – 61Combined sources3
Helixi65 – 77Combined sources13
Beta strandi82 – 86Combined sources5
Helixi89 – 91Combined sources3
Helixi92 – 100Combined sources9
Beta strandi106 – 112Combined sources7
Helixi115 – 126Combined sources12
Helixi130 – 132Combined sources3
Beta strandi133 – 138Combined sources6
Helixi140 – 149Combined sources10
Helixi151 – 153Combined sources3
Beta strandi157 – 162Combined sources6
Helixi169 – 179Combined sources11
Beta strandi186 – 189Combined sources4
Turni190 – 192Combined sources3
Helixi193 – 198Combined sources6
Helixi207 – 224Combined sources18
Beta strandi232 – 234Combined sources3
Beta strandi240 – 243Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SUIX-ray2.70A/B/C/D1-247[»]
1SUSX-ray2.70A/B/C/D1-247[»]
ProteinModelPortaliQ40313.
SMRiQ40313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ40313.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni87 – 88S-adenosyl-L-methionine binding1 Publication2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01596. Methyltransf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51682. SAM_OMT_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q40313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNEDQKQT ESGRHQEVGH KSLLQSDALY QYILETSVFP REHEAMKELR
60 70 80 90 100
EVTAKHPWNI MTTSADEGQF LSMLLKLINA KNTMEIGVYT GYSLLATALA
110 120 130 140 150
IPEDGKILAM DINKENYELG LPVIKKAGVD HKIDFREGPA LPVLDEMIKD
160 170 180 190 200
EKNHGSYDFI FVDADKDNYL NYHKRLIDLV KVGGVIGYDN TLWNGSVVAP
210 220 230 240
PDAPLRKYVR YYRDFVLELN KALAVDPRIE ICMLPVGDGI TICRRIK
Length:247
Mass (Da):27,999
Last modified:November 1, 1996 - v1
Checksum:i2B82576EB21E3DA8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20736 mRNA. Translation: AAC28973.1.
PIRiT09399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20736 mRNA. Translation: AAC28973.1.
PIRiT09399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SUIX-ray2.70A/B/C/D1-247[»]
1SUSX-ray2.70A/B/C/D1-247[»]
ProteinModelPortaliQ40313.
SMRiQ40313.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ40313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00711.
BRENDAi2.1.1.104. 3078.

Miscellaneous databases

EvolutionaryTraceiQ40313.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01596. Methyltransf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51682. SAM_OMT_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAMT_MEDSA
AccessioniPrimary (citable) accession number: Q40313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.