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Entry version 44 (07 Apr 2021)
Sequence version 1 (01 Jun 2003)
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Monomethylxanthine methyltransferase 2



Coffea arabica (Arabian coffee)
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the biosynthesis of caffeine. Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine and with a lower activity of paraxanthine to caffeine (PubMed:12746542, PubMed:12527364, PubMed:18068204).

Does not have 1-N-methylation activity (PubMed:12527364).

1 Publication2 Publications

<p>This subsection of the <a href="">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=171 µM for 7-methylxanthine2 Publications
  2. KM=251 µM for 7-methylxanthine1 Publication
  3. KM=738 µM for paraxanthine1 Publication
  4. KM=14 µM for S-adenosyl-L-methionine1 Publication

    pH dependencei

    Optimum pH is 8.2 Publications

    <p>This subsection of the <a href="">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Alkaloid biosynthesis

    This protein is involved in Alkaloid biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in Alkaloid biosynthesis.


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei18S-adenosyl-L-methionineBy similarity1
    Binding sitei18SubstrateBy similarity1
    Binding sitei60S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
    Binding sitei61S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
    Binding sitei66S-adenosyl-L-methionineBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei154Involved in substrate discriminationBy similarity1
    <p>This subsection of the <a href="">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi178Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi262Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi263MagnesiumBy similarity1
    Sitei266Involved in substrate discriminationBy similarity1
    Binding sitei333SubstrateBy similarity1
    Sitei343Involved in substrate discriminationBy similarity1
    Binding sitei368SubstrateBy similarity1

    <p>The <a href="">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionMethyltransferase, Transferase
    Biological processAlkaloid metabolism
    LigandMagnesium, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    BRENDAi, 1559

    SABIO-RK: Biochemical Reaction Kinetics Database


    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Monomethylxanthine methyltransferase 22 Publications (EC: Publications)
    Short name:
    CaMXMT22 Publications
    Alternative name(s):
    7-methylxanthine N-methyltransferase 22 Publications
    Theobromine synthase 21 Publication
    Theobromine synthase 3
    <p>This subsection of the <a href="">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:MXMT22 Publications
    Synonyms:CTS21 Publication
    <p>This subsection of the <a href="">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCoffea arabica (Arabian coffee)
    <p>This subsection of the <a href="">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri13443 [NCBI]
    <p>This subsection of the <a href="">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeIxoroideaeGardenieae complexBertiereae - Coffeeae cladeCoffeeaeCoffea
    <p>This subsection of the <a href="">Names and taxonomy</a> section is present for entries that are part of a <a href="">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000515148 <p>A UniProt <a href="">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome assembly

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004083051 – 384Monomethylxanthine methyltransferase 2Add BLAST384

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="">P92958</a>, <a href="">Q8TDN4</a>, <a href="">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed, at low levels, in young leaves, floral buds and immature fruits (grains), but not in old leaves and mature fruits (PubMed:12746542, PubMed:25249475). Highly expressed in developing endosperm and flower buds (PubMed:12527364). Detected in young leaves (PubMed:12527364, PubMed:25249475).3 Publications

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models


    Database of comparative protein structure models


    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni21 – 25Substrate bindingBy similarity5
    Regioni60 – 61S-adenosyl-L-methionine bindingBy similarity2
    Regioni98 – 101S-adenosyl-L-methionine bindingBy similarity4
    Regioni139 – 141S-adenosyl-L-methionine bindingBy similarity3
    Regioni156 – 158S-adenosyl-L-methionine bindingBy similarity3
    Regioni157 – 161Substrate bindingBy similarity5

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    1.10.1200.270, 1 hit

    Integrated resource of protein families, domains and functional sites

    View protein in InterPro
    IPR005299, MeTrfase_7
    IPR042086, MeTrfase_capping
    IPR029063, SAM-dependent_MTases

    The PANTHER Classification System

    PTHR31009, PTHR31009, 1 hit

    Pfam protein domain database

    View protein in Pfam
    PF03492, Methyltransf_7, 1 hit

    Superfamily database of structural and functional annotation

    SSF53335, SSF53335, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="">length</a> and <a href="">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="">Sequence</a> section indicates if the <a href="">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q84PP7-1 [UniParc]FASTAAdd to basket
    « Hide
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    260 270 280 290 300
    310 320 330 340 350
    360 370 380
    Mass (Da):43,472
    Last modified:June 1, 2003 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDC8FC623081280A1

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti5E → A in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti11E → G in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti11E → G in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti11E → G in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti22A → S in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti22A → S in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti22A → S in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti34F → V in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti34F → V in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti34F → V in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti52K → N in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti52K → N in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti52K → N in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti153L → I in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti153L → I in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti153L → I in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti159V → F in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti159V → F in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti159V → F in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti176G → S in AFV60440 (PubMed:25249475).Curated1
    Sequence conflicti176G → S in AFV60448 (PubMed:25249475).Curated1
    Sequence conflicti176G → S in BAC43757 (PubMed:12527364).Curated1
    Sequence conflicti384V → M in BAC43757 (PubMed:12527364).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database


    GenBank nucleotide sequence database


    DNA Data Bank of Japan; a nucleotide sequence database

    Links Updated
    AB054841 mRNA Translation: BAC43757.1
    AB084126 mRNA Translation: BAC75664.1
    JX978512 Genomic DNA Translation: AFV60440.1
    JX978520 mRNA Translation: AFV60448.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes


    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    Links Updated
    AB054841 mRNA Translation: BAC43757.1
    AB084126 mRNA Translation: BAC75664.1
    JX978512 Genomic DNA Translation: AFV60440.1
    JX978520 mRNA Translation: AFV60448.1

    3D structure databases


    Genome annotation databases


    Enzyme and pathway databases

    BRENDAi2.1.1.159, 1559

    Family and domain databases

    Gene3Di1.10.1200.270, 1 hit
    InterProiView protein in InterPro
    IPR005299, MeTrfase_7
    IPR042086, MeTrfase_capping
    IPR029063, SAM-dependent_MTases
    PANTHERiPTHR31009, PTHR31009, 1 hit
    PfamiView protein in Pfam
    PF03492, Methyltransf_7, 1 hit
    SUPFAMiSSF53335, SSF53335, 1 hit

    MobiDB: a database of protein disorder and mobility annotations


    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMXMT2_COFAR
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q84PP7
    Secondary accession number(s): A0A096VHZ2, Q8H0G0
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: June 1, 2003
    Last modified: April 7, 2021
    This is version 44 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome


    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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