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P28002

- COMT1_MEDSA

UniProt

P28002 - COMT1_MEDSA

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Protein

Caffeic acid 3-O-methyltransferase

Gene
N/A
Organism
Medicago sativa (Alfalfa)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei208 – 2081S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei231 – 2311S-adenosyl-L-methionine
Binding sitei251 – 2511S-adenosyl-L-methionine
Binding sitei252 – 2521S-adenosyl-L-methionine; via amide nitrogen
Binding sitei265 – 2651S-adenosyl-L-methionine
Active sitei269 – 2691Proton acceptor

GO - Molecular functioni

  1. caffeate O-methyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. lignin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lignin biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Caffeic acid 3-O-methyltransferasePRO_0000063204Add
BLAST

Proteomic databases

ProMEXiP28002.

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

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2712
Turni28 – 303
Helixi31 – 4111
Helixi44 – 496
Helixi59 – 646
Helixi73 – 8614
Beta strandi89 – 968
Beta strandi102 – 1087
Helixi110 – 1156
Helixi125 – 1317
Helixi134 – 1374
Helixi138 – 1425
Helixi143 – 1497
Helixi153 – 1586
Helixi162 – 1654
Helixi166 – 1683
Helixi170 – 19425
Beta strandi202 – 2076
Turni210 – 2123
Helixi213 – 2219
Beta strandi225 – 2317
Turni233 – 2375
Beta strandi245 – 2495
Turni252 – 2543
Beta strandi265 – 2684
Helixi273 – 28614
Beta strandi289 – 2913
Beta strandi293 – 2975
Helixi308 – 32316
Beta strandi324 – 3263
Helixi332 – 34211
Beta strandi347 – 3537
Beta strandi356 – 3616

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KYWX-ray2.40A/C/F1-365[»]
1KYZX-ray2.20A/C/E1-365[»]
ProteinModelPortaliP28002.
SMRiP28002. Positions 5-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28002.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 1367Substrate binding
Regioni162 – 18019Substrate bindingAdd
BLAST

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. COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF53335. 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:
EMBL
GenBank
DDBJ
Links Updated
M63853 mRNA. Translation: AAB46623.1.
PIRiT09673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63853 mRNA. Translation: AAB46623.1 .
PIRi T09673.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KYW X-ray 2.40 A/C/F 1-365 [» ]
1KYZ X-ray 2.20 A/C/E 1-365 [» ]
ProteinModelPortali P28002.
SMRi P28002. Positions 5-365.
ModBasei Search...
MobiDBi Search...

Proteomic databases

ProMEXi P28002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00711 .

Miscellaneous databases

EvolutionaryTracei P28002.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProi IPR016461. COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF005739. O-mtase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51683. SAM_OMT_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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."
    Gowri G., Bugos R.C., Campbell W.H., Maxwell C.A., Dixon R.A.
    Plant Physiol. 97:7-14(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Apollo.
  2. "Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase."
    Zubieta C., Kota P., Ferrer J.-L., Dixon R.A., Noel J.P.
    Plant Cell 14:1265-1277(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, SUBUNIT.

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: October 1, 2014
This is version 77 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

External Data

Dasty 3