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Protein

Caffeic acid 3-O-methyltransferase

Gene
N/A
Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid. The resulting products may subsequently be converted to the corresponding alcohols that are incorporated into lignins.

Catalytic activityi

S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate.

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 sitei131SubstrateCombined sources1 Publication1
Binding sitei208S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Binding sitei231S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Binding sitei251S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei252S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1
Binding sitei265S-adenosyl-L-methionineCombined sources1 Publication1
Active sitei269Proton acceptorPROSITE-ProRule annotationCombined sources1 Publication1
Active sitei297By similarity1
Active sitei329By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lignin biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.68. 3078.
UniPathwayiUPA00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Caffeic acid 3-O-methyltransferase (EC:2.1.1.68)
Short name:
CAOMT
Short name:
COMT
Alternative name(s):
S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000632041 – 365Caffeic acid 3-O-methyltransferaseAdd BLAST365

Proteomic databases

PRIDEiP28002.

Expressioni

Tissue specificityi

More abundant in roots and stems.

Inductioni

By infection, plant wounding, or elicitor treatment of cell cultures.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 27Combined sources12
Turni28 – 30Combined sources3
Helixi31 – 41Combined sources11
Helixi44 – 49Combined sources6
Helixi59 – 64Combined sources6
Helixi73 – 86Combined sources14
Beta strandi89 – 96Combined sources8
Beta strandi102 – 108Combined sources7
Helixi110 – 115Combined sources6
Helixi125 – 131Combined sources7
Helixi134 – 137Combined sources4
Helixi138 – 142Combined sources5
Helixi143 – 149Combined sources7
Helixi153 – 158Combined sources6
Helixi162 – 165Combined sources4
Helixi166 – 168Combined sources3
Helixi170 – 194Combined sources25
Beta strandi202 – 207Combined sources6
Turni210 – 212Combined sources3
Helixi213 – 221Combined sources9
Beta strandi225 – 231Combined sources7
Turni233 – 237Combined sources5
Beta strandi245 – 249Combined sources5
Turni252 – 254Combined sources3
Beta strandi265 – 268Combined sources4
Helixi273 – 286Combined sources14
Beta strandi289 – 291Combined sources3
Beta strandi293 – 297Combined sources5
Helixi308 – 323Combined sources16
Beta strandi324 – 326Combined sources3
Helixi332 – 342Combined sources11
Beta strandi347 – 353Combined sources7
Beta strandi356 – 361Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KYWX-ray2.40A/C/F1-365[»]
1KYZX-ray2.20A/C/E1-365[»]
ProteinModelPortaliP28002.
SMRiP28002.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28002.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni130 – 136Substrate binding7
Regioni162 – 180Substrate bindingAdd BLAST19

Sequence similaritiesi

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

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTGETQIT PTHISDEEAN LFAMQLASAS VLPMILKSAL ELDLLEIIAK
60 70 80 90 100
AGPGAQISPI EIASQLPTTN PDAPVMLDRM LRLLACYIIL TCSVRTQQDG
110 120 130 140 150
KVQRLYGLAT VAKYLVKNED GVSISALNLM NQDKVLMESW YHLKDAVLDG
160 170 180 190 200
GIPFNKAYGM TAFEYHGTDP RFNKVFNKGM SDHSTITMKK ILETYTGFEG
210 220 230 240 250
LKSLVDVGGG TGAVINTIVS KYPTIKGINF DLPHVIEDAP SYPGVEHVGG
260 270 280 290 300
DMFVSIPKAD AVFMKWICHD WSDEHCLKFL KNCYEALPDN GKVIVAECIL
310 320 330 340 350
PVAPDSSLAT KGVVHIDVIM LAHNPGGKER TQKEFEDLAK GAGFQGFKVH
360
CNAFNTYIME FLKKV
Length:365
Mass (Da):39,946
Last modified:August 1, 1992 - v1
Checksum:iC14B0D75F979C6B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63853 mRNA. Translation: AAB46623.1.
PIRiT09673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63853 mRNA. Translation: AAB46623.1.
PIRiT09673.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KYWX-ray2.40A/C/F1-365[»]
1KYZX-ray2.20A/C/E1-365[»]
ProteinModelPortaliP28002.
SMRiP28002.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP28002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00711.
BRENDAi2.1.1.68. 3078.

Miscellaneous databases

EvolutionaryTraceiP28002.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOMT1_MEDSA
AccessioniPrimary (citable) accession number: P28002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 2016
This is version 86 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.