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P28002

- COMT1_MEDSA

UniProt

P28002 - COMT1_MEDSA

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
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    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

    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

    MGSTGETQIT PTHISDEEAN LFAMQLASAS VLPMILKSAL ELDLLEIIAK    50
    AGPGAQISPI EIASQLPTTN PDAPVMLDRM LRLLACYIIL TCSVRTQQDG 100
    KVQRLYGLAT VAKYLVKNED GVSISALNLM NQDKVLMESW YHLKDAVLDG 150
    GIPFNKAYGM TAFEYHGTDP RFNKVFNKGM SDHSTITMKK ILETYTGFEG 200
    LKSLVDVGGG TGAVINTIVS KYPTIKGINF DLPHVIEDAP SYPGVEHVGG 250
    DMFVSIPKAD AVFMKWICHD WSDEHCLKFL KNCYEALPDN GKVIVAECIL 300
    PVAPDSSLAT KGVVHIDVIM LAHNPGGKER TQKEFEDLAK GAGFQGFKVH 350
    CNAFNTYIME FLKKV 365
    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