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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211Substrate; via amide nitrogen1 Publication
Binding sitei63 – 631S-adenosyl-L-methionine; via amide nitrogen1 Publication
Binding sitei85 – 851S-adenosyl-L-methionine1 Publication
Binding sitei93 – 931S-adenosyl-L-methionine1 Publication
Binding sitei111 – 1111S-adenosyl-L-methionine1 Publication
Binding sitei140 – 1401S-adenosyl-L-methionine; via amide nitrogen1 Publication
Metal bindingi163 – 1631Divalent metal cation1 Publication
Binding sitei163 – 1631Substrate1 Publication
Binding sitei165 – 1651S-adenosyl-L-methionine1 Publication
Metal bindingi189 – 1891Divalent metal cation1 Publication
Metal bindingi190 – 1901Divalent metal cation1 Publication
Binding sitei194 – 1941Substrate1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Caffeoyl-CoA O-methyltransferasePRO_0000165686Add
BLAST

Proteomic databases

PRIDEiQ40313.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Helixi27 – 3711Combined sources
Beta strandi39 – 413Combined sources
Helixi45 – 5410Combined sources
Helixi59 – 613Combined sources
Helixi65 – 7713Combined sources
Beta strandi82 – 865Combined sources
Helixi89 – 913Combined sources
Helixi92 – 1009Combined sources
Beta strandi106 – 1127Combined sources
Helixi115 – 12612Combined sources
Helixi130 – 1323Combined sources
Beta strandi133 – 1386Combined sources
Helixi140 – 14910Combined sources
Helixi151 – 1533Combined sources
Beta strandi157 – 1626Combined sources
Helixi169 – 17911Combined sources
Beta strandi186 – 1894Combined sources
Turni190 – 1923Combined sources
Helixi193 – 1986Combined sources
Helixi207 – 22418Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi240 – 2434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SUIX-ray2.70A/B/C/D1-247[»]
1SUSX-ray2.70A/B/C/D1-247[»]
ProteinModelPortaliQ40313.
SMRiQ40313. Positions 21-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ40313.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 882S-adenosyl-L-methionine binding1 Publication

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1SUIX-ray2.70A/B/C/D1-247[»]
1SUSX-ray2.70A/B/C/D1-247[»]
ProteinModelPortaliQ40313.
SMRiQ40313. Positions 21-247.
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: January 20, 2016
This is version 80 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.