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Protein

Isoliquiritigenin 2'-O-methyltransferase

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

Functioni

Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin.2 Publications
S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine + 2'-O-methyllicodione.1 Publication

Enzyme regulationi

Inhibited by 1 mM Co2+, Cu2+, Zn2+ or Fe2+. Non-competitively inhibited by S-adenosyl-L-homocysteine. Competitively inhibited by 2'-O-methylisoliquiritigenin.1 Publication

Kineticsi

  1. KM=2.2 µM for isoliquiritigenin1 Publication
  2. KM=17.7 µM for S-adenosyl-L-methionine1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei217 – 2171S-adenosyl-L-methionine; via carbonyl oxygen
    Binding sitei240 – 2401S-adenosyl-L-methionine
    Binding sitei260 – 2601S-adenosyl-L-methionine
    Binding sitei261 – 2611S-adenosyl-L-methionine; via amide nitrogen
    Binding sitei274 – 2741S-adenosyl-L-methionine
    Active sitei278 – 2781Proton acceptorPROSITE-ProRule annotation1 Publication

    GO - Molecular functioni

    • isoliquiritigenin 2'-O-methyltransferase activity Source: UniProtKB
    • licodione 2'-O-methyltransferase activity Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    SABIO-RKP93324.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoliquiritigenin 2'-O-methyltransferase (EC:2.1.1.1542 Publications)
    Short name:
    MsCHMT
    Alternative name(s):
    Chalcone O-methyltransferase
    Short name:
    ChOMT
    Licodione 2'-O-methyltransferase (EC:2.1.1.651 Publication)
    Short name:
    MsLMT
    OrganismiMedicago sativa (Alfalfa)
    Taxonomic identifieri3879 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 372371Isoliquiritigenin 2'-O-methyltransferasePRO_0000204439Add
    BLAST

    Expressioni

    Tissue specificityi

    Roots (at protein level). Expressed mainly in roots, and to a lesser extent in root nodules. In the roots, expression is not detected in the root tip or the cells immediately behind the tip, but is detected in tissues starting 1.5-2.0 mm distal to the root tip. Detected in the epidermal and cortical cells of 2 day old roots, with lower levels in vascular tissue.3 Publications

    Developmental stagei

    Levels are highest one week after planting.1 Publication

    Inductioni

    By fungal elicitor.1 Publication

    Interactioni

    Subunit structurei

    Monomer (PubMed:1731632). Homodimer (PubMed:11224575).2 Publications

    Structurei

    Secondary structure

    1
    372
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 3313Combined sources
    Helixi36 – 4611Combined sources
    Helixi49 – 546Combined sources
    Helixi65 – 695Combined sources
    Helixi74 – 763Combined sources
    Helixi81 – 9414Combined sources
    Beta strandi97 – 1048Combined sources
    Beta strandi110 – 1167Combined sources
    Helixi120 – 1234Combined sources
    Helixi134 – 1396Combined sources
    Helixi142 – 1487Combined sources
    Helixi151 – 1566Combined sources
    Helixi179 – 20325Combined sources
    Turni206 – 2094Combined sources
    Beta strandi211 – 2166Combined sources
    Helixi222 – 2309Combined sources
    Beta strandi235 – 2406Combined sources
    Helixi242 – 2454Combined sources
    Beta strandi254 – 2585Combined sources
    Turni261 – 2633Combined sources
    Beta strandi268 – 2769Combined sources
    Helixi277 – 2793Combined sources
    Helixi282 – 29514Combined sources
    Beta strandi296 – 30914Combined sources
    Helixi317 – 33317Combined sources
    Helixi340 – 34910Combined sources
    Beta strandi353 – 3619Combined sources
    Turni362 – 3643Combined sources
    Beta strandi365 – 3717Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FP1X-ray1.82D1-372[»]
    1FPQX-ray2.00A1-372[»]
    ProteinModelPortaliP93324.
    SMRiP93324. Positions 19-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP93324.

    Family & Domainsi

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P93324-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGNSYITKED NQISATSEQT EDSACLSAMV LTTNLVYPAV LNAAIDLNLF
    60 70 80 90 100
    EIIAKATPPG AFMSPSEIAS KLPASTQHSD LPNRLDRMLR LLASYSVLTS
    110 120 130 140 150
    TTRTIEDGGA ERVYGLSMVG KYLVPDESRG YLASFTTFLC YPALLQVWMN
    160 170 180 190 200
    FKEAVVDEDI DLFKNVHGVT KYEFMGKDKK MNQIFNKSMV DVCATEMKRM
    210 220 230 240 250
    LEIYTGFEGI STLVDVGGGS GRNLELIISK YPLIKGINFD LPQVIENAPP
    260 270 280 290 300
    LSGIEHVGGD MFASVPQGDA MILKAVCHNW SDEKCIEFLS NCHKALSPNG
    310 320 330 340 350
    KVIIVEFILP EEPNTSEESK LVSTLDNLMF ITVGGRERTE KQYEKLSKLS
    360 370
    GFSKFQVACR AFNSLGVMEF YK
    Length:372
    Mass (Da):41,138
    Last modified:May 1, 1997 - v1
    Checksum:i3ADC2D65E33F240E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L10211 mRNA. Translation: AAB48059.1.
    PIRiT09617.

    Genome annotation databases

    KEGGiag:AAB48059.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L10211 mRNA. Translation: AAB48059.1.
    PIRiT09617.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FP1X-ray1.82D1-372[»]
    1FPQX-ray2.00A1-372[»]
    ProteinModelPortaliP93324.
    SMRiP93324. Positions 19-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAB48059.

    Enzyme and pathway databases

    SABIO-RKP93324.

    Miscellaneous databases

    EvolutionaryTraceiP93324.

    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...

    Publicationsi

    1. "Molecular characterization and expression of alfalfa isoliquiritigenin 2'-O-methyltransferase, an enzyme specifically involved in the biosynthesis of an inducer of Rhizobium meliloti nodulation genes."
      Maxwell C.A., Harrison M.J., Dixon R.A.
      Plant J. 4:971-981(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: cv. Apollo.
    2. "Identification, purification, and characterization of S-adenosyl-L-methionine: isoliquiritigenin 2'-O-methyltransferase from alfalfa (Medicago sativa L.)."
      Maxwell C.A., Edwards R., Dixon R.A.
      Arch. Biochem. Biophys. 293:158-166(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY.
      Strain: cv. Apollo.
    3. "Enzymic O-methylation of isoliquiritigenin and licodione in alfalfa and licorice cultures."
      Ichimura M., Furuno T., Takahashi T., Dixon R.A., Ayabe S.
      Phytochemistry 44:991-995(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      Strain: cv. Moapa.
    4. "Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases."
      Zubieta C., He X.-Z., Dixon R.A., Noel J.P.
      Nat. Struct. Biol. 8:271-279(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, SUBUNIT, SUBSTRATE-BINDING, ACTIVE SITE.
      Strain: cv. Apollo.

    Entry informationi

    Entry nameiCHOMT_MEDSA
    AccessioniPrimary (citable) accession number: P93324
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: May 1, 1997
    Last modified: May 11, 2016
    This is version 81 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.