[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Apollo; PubMed=16668418 [NCBI, ExPASy, EBI, Israel, Japan] Gowri G., Bugos R.C., Campbell W.H., Maxwell C.A., Dixon R.A.; "Stress responses in alfalfa (Medicago sativa L). X. Molecular cloning and expression of S-adenosyl-L-methionine:caffeic acid 3-O-methyltransferase, a key enzyme of lignin biosynthesis."; Plant Physiol. 97:7-14(1991).
[2]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND SUBUNIT. DOI=10.1105/tpc.001412; PubMed=12084826 [NCBI, ExPASy, EBI, Israel, Japan] Zubieta C., Kota P., Ferrer J.-L., Dixon R.A., Noel J.P.; "Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase."; Plant Cell 14:1265-1277(2002).

Comments

FUNCTION: 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 ACTIVITY: S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate.
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis .
SUBUNIT: Homodimer.
TISSUE SPECIFICITY: More abundant in roots and stems.
INDUCTION: By infection, plant wounding, or elicitor treatment of cell cultures.
SIMILARITY: Belongs to the methyltransferase superfamily. Type 2 family. COMT subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M63853; AAB46623.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09673; T09673.

3D structure databases

PDB

1KYW; X-ray; 2.40 A; A/C/F=1-365.	[ExPASy / RCSB / EBI]
1KYZ; X-ray; 2.20 A; A/C/E=1-365.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1KYW; -.
1KYZ; -.

ModBase

P28002.

Ontologies

GO:0047763;	Molecular function: caffeate O-methyltransferase activity (inferred from electronic annotation from EC).
GO:0046983;	Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0009809;	Biological process: lignin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016461; O-MeTrfase_COMT_euk.
IPR001077; O_MeTrfase_2.
IPR012967; Plant_MeTrfase_dimerisation.
Graphical view of domain structure.

Pfam

PF08100; Dimerisation; 1.
PF00891; Methyltransf_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005739; O-mtase; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Lignin biosynthesis; Methyltransferase; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 365`	`365`	`Caffeic acid 3-O-methyltransferase.`	`PRO_0000063204`
`REGION`	`130 136`	`7`	`Substrate binding.`
`REGION`	`162 180`	`19`	`Substrate binding.`
`ACT_SITE`	`269 269`		`Proton acceptor.`
`BINDING`	`208 208`		`S-adenosyl-L-methionine; via carbonyl oxygen.`
`BINDING`	`231 231`		`S-adenosyl-L-methionine.`
`BINDING`	`251 251`		`S-adenosyl-L-methionine.`
`BINDING`	`252 252`		`S-adenosyl-L-methionine; via amide nitrogen.`
`BINDING`	`265 265`		`S-adenosyl-L-methionine.`
`HELIX`	`16 27`	`12`
`TURN`	`28 30`	`3`
`HELIX`	`31 42`	`12`
`HELIX`	`44 49`	`6`
`HELIX`	`59 63`	`5`
`HELIX`	`73 86`	`14`
`STRAND`	`89 96`	`8`
`STRAND`	`102 108`	`7`
`HELIX`	`110 114`	`5`
`HELIX`	`125 131`	`7`
`HELIX`	`134 140`	`7`
`HELIX`	`143 149`	`7`
`HELIX`	`153 158`	`6`
`HELIX`	`162 168`	`7`
`HELIX`	`170 191`	`22`
`TURN`	`192 194`	`3`
`STRAND`	`202 207`	`6`
`TURN`	`210 212`	`3`
`HELIX`	`214 221`	`8`
`STRAND`	`225 231`	`7`
`HELIX`	`233 236`	`4`
`STRAND`	`245 249`	`5`
`TURN`	`252 254`	`3`
`STRAND`	`265 267`	`3`
`HELIX`	`268 270`	`3`
`HELIX`	`273 286`	`14`
`STRAND`	`289 291`	`3`
`STRAND`	`293 297`	`5`
`HELIX`	`308 323`	`16`
`STRAND`	`324 326`	`3`
`HELIX`	`332 341`	`10`
`STRAND`	`347 353`	`7`
`STRAND`	`356 361`	`6`

Sequence information

Length: 365 AA [This is the length of the unprocessed precursor]

Molecular weight: 39946 Da [This is the MW of the unprocessed precursor]

CRC64: C14B0D75F979C6B6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSTGETQIT PTHISDEEAN LFAMQLASAS VLPMILKSAL ELDLLEIIAK AGPGAQISPI 

        70         80         90        100        110        120 
EIASQLPTTN PDAPVMLDRM LRLLACYIIL TCSVRTQQDG KVQRLYGLAT VAKYLVKNED 

       130        140        150        160        170        180 
GVSISALNLM NQDKVLMESW YHLKDAVLDG GIPFNKAYGM TAFEYHGTDP RFNKVFNKGM 

       190        200        210        220        230        240 
SDHSTITMKK ILETYTGFEG LKSLVDVGGG TGAVINTIVS KYPTIKGINF DLPHVIEDAP 

       250        260        270        280        290        300 
SYPGVEHVGG DMFVSIPKAD AVFMKWICHD WSDEHCLKFL KNCYEALPDN GKVIVAECIL 

       310        320        330        340        350        360 
PVAPDSSLAT KGVVHIDVIM LAHNPGGKER TQKEFEDLAK GAGFQGFKVH CNAFNTYIME 


FLKKV

P28002 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools