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Q9FK25

- OMT1_ARATH

UniProt

Q9FK25 - OMT1_ARATH

Protein

Flavone 3'-O-methyltransferase 1

Gene

OMT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Methylates OH residues of flavonoid compounds. Converts quercetin into isorhamnetin. Dihydroquercetin is not a substrate. Catalyzes the methylation of monolignols, the lignin precursors. Does not contribute to the phenylpropanoid pattern of the pollen tryphine, but is probably confined to isorhamnetin gylcoside biosynthesis.4 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + 3'-hydroxyflavone = S-adenosyl-L-homocysteine + 3'-methoxyflavone.1 Publication
    S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate.1 Publication

    Enzyme regulationi

    Does not require magnesium. Completely inhibited by 5 mM of either NiSO4 or p-chloromercuribenzoate (pCMB).1 Publication

    Kineticsi

    1. KM=1.76 µM for quercetin (at 30 degrees Celsius, PubMed:10700397)2 Publications
    2. KM=3.38 µM for myricetin (at 30 degrees Celsius, PubMed:10700397)2 Publications
    3. KM=24.2 µM for caffeic acid (at pH 7.5, PubMed:20652169)2 Publications
    4. KM=32 µM for 5-OH ferulic acid (at pH 7.5, PubMed:20652169)2 Publications
    5. KM=19.7 µM for caffeyl aldehyde (at pH 7.5, PubMed:20652169)2 Publications
    6. KM=17.9 µM for 5-OH coniferyl aldehyde (at pH 7.5, PubMed:20652169)2 Publications
    7. KM=51.5 µM for caffeyl alcohol (at pH 7.5, PubMed:20652169)2 Publications
    8. KM=31.6 µM for 5-OH coniferyl alcohol (at pH 7.5, PubMed:20652169)2 Publications
    9. KM=23.7 µM for quercetin (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=384.6 pmol/sec/mg enzyme with quercetin as substrate2 Publications

    Vmax=227.3 pmol/sec/mg enzyme with myricetin as substrate2 Publications

    Vmax=3.8 pmol/sec/µg enzyme with quercetin as substrate (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=51.9 pmol/sec/µg enzyme with 5-OH coniferyl alcohol as substrate (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=35.3 pmol/sec/µg enzyme with caffeyl alcohol as substrate (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=66.2 pmol/sec/µg enzyme with 5-OH coniferyl aldehyde as substrate (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=35.9 pmol/sec/µg enzyme with caffeyl aldehyde as substrate (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=30.1 pmol/sec/µg enzyme with 5-OH ferulic acid as substrate (at pH 7.5, PubMed:20652169)2 Publications

    Vmax=14.6 pmol/sec/µg enzyme with caffeic acid as substrate (at pH 7.5, PubMed:20652169)2 Publications

    pH dependencei

    Optimum pH is 7.5.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei206 – 2061S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei229 – 2291S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei249 – 2491S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei250 – 2501S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei263 – 2631S-adenosyl-L-methioninePROSITE-ProRule annotation
    Active sitei267 – 2671Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. caffeate O-methyltransferase activity Source: TAIR
    2. luteolin O-methyltransferase activity Source: UniProtKB
    3. myricetin 3'-O-methyltransferase activity Source: TAIR
    4. quercetin 3-O-methyltransferase activity Source: TAIR

    GO - Biological processi

    1. flavonol biosynthetic process Source: TAIR
    2. lignin biosynthetic process Source: TAIR

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.76. 399.
    UniPathwayiUPA00724.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flavone 3'-O-methyltransferase 1 (EC:2.1.1.42)
    Short name:
    AtOMT1
    Alternative name(s):
    Caffeate O-methyltransferase 1 (EC:2.1.1.68)
    Quercetin 3'-O-methyltransferase 1
    Gene namesi
    Name:OMT1
    Synonyms:COMT1
    Ordered Locus Names:At5g54160
    ORF Names:K18G13.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G54160.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. nucleus Source: TAIR
    3. plasma membrane Source: TAIR
    4. plasmodesma Source: TAIR

    Pathology & Biotechi

    Disruption phenotypei

    Reduced levels of syringyl (S) units in lignins that contain more 5-hydroxyguaiacyl units (5-OH-G), the precursors of S-units. Substitution of sinapyl (S) alcohol-derived substructures by 5-hydroxyconiferyl alcohol (5OHG)-derived moieties in fiber cell walls. No effect on hydroxycinnamic acid amides in pollen.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 363363Flavone 3'-O-methyltransferase 1PRO_0000063217Add
    BLAST

    Proteomic databases

    PaxDbiQ9FK25.
    PRIDEiQ9FK25.

    Expressioni

    Tissue specificityi

    Expressed in seedlings, leaves, stems, flowers and siliques, mostly in vascular tissues. Mostly expressed in the apical part of the stems and in roots. Expressed in the endothecium and the epidermal anther, but not in the tapetum. Also detected in all epidermal tissues of flower organs, including petals, sepals and the tip of the stigma.2 Publications

    Developmental stagei

    Observed in young seedling and progressively restricted to vascular tissues. Present in whole blade of young leaves but confined to the vascular tissues of mature leaves. In stems, mostly present in xylem, mature phloem and differentiating fibers. In siliques, only present in the lignified extremities. Expressed during early and late stages of flower development.2 Publications

    Gene expression databases

    GenevestigatoriQ9FK25.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRL1Q9ZPS91EBI-1633761,EBI-2292728
    GRF6P483491EBI-1633761,EBI-1633785

    Protein-protein interaction databases

    BioGridi20748. 2 interactions.
    IntActiQ9FK25. 4 interactions.
    MINTiMINT-8066865.

    Structurei

    Secondary structure

    1
    363
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 143
    Helixi20 – 234
    Turni29 – 313
    Helixi32 – 365
    Turni40 – 423
    Helixi45 – 506
    Helixi57 – 604
    Beta strandi63 – 686
    Helixi74 – 785
    Helixi81 – 844
    Beta strandi85 – 873
    Beta strandi90 – 923
    Beta strandi96 – 983
    Beta strandi102 – 1043
    Turni111 – 1133
    Beta strandi117 – 1193
    Helixi125 – 1284
    Beta strandi135 – 1373
    Helixi142 – 1454
    Helixi151 – 1555
    Helixi160 – 1667
    Helixi168 – 19225
    Beta strandi200 – 2045
    Beta strandi208 – 2103
    Turni213 – 2164
    Beta strandi221 – 2299
    Turni231 – 2333
    Beta strandi243 – 2486
    Beta strandi250 – 2523
    Beta strandi258 – 2658
    Turni266 – 2683
    Helixi273 – 28311
    Beta strandi290 – 2956
    Helixi306 – 3094
    Helixi314 – 3207
    Beta strandi322 – 3243
    Helixi330 – 34011
    Beta strandi343 – 3508
    Beta strandi355 – 3606

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NIImodel-A1-363[»]
    ProteinModelPortaliQ9FK25.
    SMRiQ9FK25. Positions 10-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0500.
    HOGENOMiHOG000238276.
    InParanoidiQ9FK25.
    KOiK05279.
    OMAiCRTEESK.
    PhylomeDBiQ9FK25.

    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.

    Q9FK25-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSTAETQLT PVQVTDDEAA LFAMQLASAS VLPMALKSAL ELDLLEIMAK    50
    NGSPMSPTEI ASKLPTKNPE APVMLDRILR LLTSYSVLTC SNRKLSGDGV 100
    ERIYGLGPVC KYLTKNEDGV SIAALCLMNQ DKVLMESWYH LKDAILDGGI 150
    PFNKAYGMSA FEYHGTDPRF NKVFNNGMSN HSTITMKKIL ETYKGFEGLT 200
    SLVDVGGGIG ATLKMIVSKY PNLKGINFDL PHVIEDAPSH PGIEHVGGDM 250
    FVSVPKGDAI FMKWICHDWS DEHCVKFLKN CYESLPEDGK VILAECILPE 300
    TPDSSLSTKQ VVHVDCIMLA HNPGGKERTE KEFEALAKAS GFKGIKVVCD 350
    AFGVNLIELL KKL 363
    Length:363
    Mass (Da):39,618
    Last modified:March 1, 2001 - v1
    Checksum:iB4380028D89C43DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291D → N in AAB96879. (PubMed:9349713)Curated
    Sequence conflicti295 – 2951E → V in CAA81580. (PubMed:8580968)Curated
    Sequence conflicti301 – 3011T → S in CAA81580. (PubMed:8580968)Curated
    Sequence conflicti348 – 3481V → C in CAA81580. (PubMed:8580968)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70424 mRNA. Translation: AAB96879.1.
    AB013387 Genomic DNA. Translation: BAB11578.1.
    CP002688 Genomic DNA. Translation: AED96460.1.
    AY062837 mRNA. Translation: AAL32915.1.
    AY081565 mRNA. Translation: AAM10127.1.
    AY087297 mRNA. Translation: AAM64849.1.
    Z27062 mRNA. Translation: CAA81580.1.
    RefSeqiNP_200227.1. NM_124796.3.
    UniGeneiAt.47593.
    At.72792.
    At.74847.

    Genome annotation databases

    EnsemblPlantsiAT5G54160.1; AT5G54160.1; AT5G54160.
    GeneIDi835504.
    KEGGiath:AT5G54160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70424 mRNA. Translation: AAB96879.1 .
    AB013387 Genomic DNA. Translation: BAB11578.1 .
    CP002688 Genomic DNA. Translation: AED96460.1 .
    AY062837 mRNA. Translation: AAL32915.1 .
    AY081565 mRNA. Translation: AAM10127.1 .
    AY087297 mRNA. Translation: AAM64849.1 .
    Z27062 mRNA. Translation: CAA81580.1 .
    RefSeqi NP_200227.1. NM_124796.3.
    UniGenei At.47593.
    At.72792.
    At.74847.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NII model - A 1-363 [» ]
    ProteinModelPortali Q9FK25.
    SMRi Q9FK25. Positions 10-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 20748. 2 interactions.
    IntActi Q9FK25. 4 interactions.
    MINTi MINT-8066865.

    Proteomic databases

    PaxDbi Q9FK25.
    PRIDEi Q9FK25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G54160.1 ; AT5G54160.1 ; AT5G54160 .
    GeneIDi 835504.
    KEGGi ath:AT5G54160.

    Organism-specific databases

    TAIRi AT5G54160.

    Phylogenomic databases

    eggNOGi COG0500.
    HOGENOMi HOG000238276.
    InParanoidi Q9FK25.
    KOi K05279.
    OMAi CRTEESK.
    PhylomeDBi Q9FK25.

    Enzyme and pathway databases

    UniPathwayi UPA00724 .
    BRENDAi 2.1.1.76. 399.

    Miscellaneous databases

    PROi Q9FK25.

    Gene expression databases

    Genevestigatori Q9FK25.

    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. "An Arabidopsis gene encoding a putative 14-3-3-interacting protein, caffeic acid/5-hydroxyferulic acid O-methyltransferase."
      Zhang H., Wang J., Goodman H.M.
      Biochim. Biophys. Acta 1353:199-202(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. C24.
      Tissue: Leaf.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
      Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
      DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-363.
      Strain: cv. Columbia.
      Tissue: Green siliques.
    7. "Functional expression of an Arabidopsis cDNA clone encoding a flavonol 3'-O-methyltransferase and characterization of the gene product."
      Muzac I., Wang J., Anzellotti D., Zhang H., Ibrahim R.K.
      Arch. Biochem. Biophys. 375:385-388(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    8. "A new Arabidopsis thaliana mutant deficient in the expression of O-methyltransferase impacts lignins and sinapoyl esters."
      Goujon T., Sibout R., Pollet B., Maba B., Nussaume L., Bechtold N., Lu F., Ralph J., Mila I., Barriere Y., Lapierre C., Jouanin L.
      Plant Mol. Biol. 51:973-989(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: cv. Wassilewskija.
    9. "Insights into lignin primary structure and deconstruction from Arabidopsis thaliana COMT (caffeic acid O-methyl transferase) mutant Atomt1."
      Moinuddin S.G.A., Jourdes M., Laskar D.D., Ki C., Cardenas C.L., Kim K.-W., Zhang D., Davin L.B., Lewis N.G.
      Org. Biomol. Chem. 8:3928-3946(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: cv. Wassilewskija.
    10. "The role of CCoAOMT1 and COMT1 in Arabidopsis anthers."
      Fellenberg C., van Ohlen M., Handrick V., Vogt T.
      Planta 236:51-61(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    11. "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
      Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
      Plant Physiol. Biochem. 0:0-0(2013)
      Cited for: REVIEW, NOMENCLATURE.
    12. "The three-dimensional structure of Arabidopsis thaliana O-methyltransferase predicted by homology-based modelling."
      Yang H., Ahn J.-H., Ibrahim R.K., Lee S., Lim Y.
      J. Mol. Graph. Model. 23:77-87(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiOMT1_ARATH
    AccessioniPrimary (citable) accession number: Q9FK25
    Secondary accession number(s): O49964, Q42170
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 108 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, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3