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Reviewed, UniProtKB/Swiss-Prot Q42653 (OMT2_CHRAE)

Last modified January 20, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Quercetin 3-O-methyltransferase 2
    EC=2.1.1.76
Alternative name(s):
    Flavonol 3-O-methyltransferase 2
Gene names
Name: OMT2
OrganismChrysosplenium americanum (Golden saxifrage)
Taxonomic identifier36749 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsSaxifragalesSaxifragaceaeChrysosplenium

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Methylates OH residues of flavonoid and phenylpropanoid compounds and shows a higher affinity for flavonoid than phenylpropanoid substrates. Substrate preference is quercetin (flavonoid) = luteolin (flavonoid) = 5-hydroxyferulic acid (phenylpropanoid) > caffeic acid (phenylpropanoid) >> apigenin (flavonoid) = kempferol (flavonoid). 3,4-dimethylquercetin is not a substrate.

Catalytic activity

S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxyflavone.

Pathway

Flavonoid metabolism; quercetin degradation.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the methyltransferase superfamily. Type 2 family. COMT subfamily.

Caution

It is not sure if OMT1 and OMT2 are really encoded by two different genes or if they represent cloning artifacts.

biophysicochemical properties

Kinetic parameters:

The Vmax value for flavonoid compounds methylation is two to threefold lower for OMT2 than for OMT1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Quercetin 3-O-methyltransferase 2
PRO_0000063216

Sites

Active site2451Proton acceptor By similarity
Binding site1841S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2071S-adenosyl-L-methionine By similarity
Binding site2271S-adenosyl-L-methionine By similarity
Binding site2281S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site2411S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42653-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8D363A98330FDE4F

FASTA34337,868
        10         20         30         40         50         60 
MLFAMQLACA SVLPMVLKSA IELDLLEIIR GQDTCMSPTE IASHLPTTNP DAPAMVDRIL 

        70         80         90        100        110        120 
RLLSCYSVVT CSVRSVDDQR VYGLAPVCKY LTKNQDGVSI AALCLMNQDK VLMESWYHLK 

       130        140        150        160        170        180 
DAVLDGGIPF NKAYGMSSFE YHGTDPRFNK VFNRGMSDHS TITMKKVFQT YQGFQGLTSL 

       190        200        210        220        230        240 
VDVGGGTGAT LTMILSKYPT IRCINFDLPH VIEDAPEYPG IEHVGGDMFV SVPKGDAIFM 

       250        260        270        280        290        300 
KWICHDWSDE HCLKLLKNCY DALPNNGKVI LAECILPEVP DSSLATKGVV HIDVITVAHN 

       310        320        330        340 
PGGKERTEKE FEALAKAAGF QGFQVFCNAF NTYIIEFSKK ICN 

« Hide

References

[1]"Characterization of two cDNA clones which encode O-methyltransferases for the methylation of both flavonoid and phenylpropanoid compounds."
Gauthier A., Gulick P.J., Ibrahim R.K.
Arch. Biochem. Biophys. 351:243-249(1998) [PubMed: 9514654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Leaf.

Cross-references

Sequence databases

U16793 mRNA. Translation: AAA86982.1.

3D structure databases

HSSPHSSP built from PDB template 1KYZ based on UniProtKB P28002.
SMRQ42653. Positions 2-341.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.1.1.76. 262661.

Family and domain databases

InterProIPR016461. O-MeTrfase_COMT_euk.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFPIRSF005739. O-mtase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameOMT2_CHRAE
AccessionPrimary (citable) accession number: Q42653
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: November 1, 1996
Last modified: January 20, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents