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Entry version 8 (02 Jun 2021)
Sequence version 1 (13 Nov 2019)
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Protein

L-tyrosine decarboxylase

Gene

tyrDC

Organism
Enterococcus faecalis (strain EnGen0310 / MMH594)
Status
Reviewed-Annotation score:

Annotation score:5 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

Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:31196984).

Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecalis (By similarity).

By similarity1 Publication

Also involved in drug metabolism, being able to catalyze decarboxylation of levodopa (L-dopa) to dopamine. In gut microbiota this enzyme is in fact exclusively responsible for the decarboxylation of levodopa, and thus reduces in situ levels of levodopa in the treatment of Parkinson's disease. It was shown that abundance of bacterial tyrosine decarboxylase in the proximal small intestine - the primary site of levodopa absorption - contributes to interindividual variation in drug efficacy and can explain the requirement for an increased dosage regimen of levodopa treatment in Parkinson's disease patients.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

pyridoxal 5'-phosphate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

(S)-alpha-fluoromethyltyrosine (AFMT) specifically inhibits microbial L-dopa decarboxylase activity, including in Parkinson's disease patient microbiotas. AFMT shows potential to block degradation of L-dopa by E.faecalis in mice. Blocking bacterial L-dopa decarboxylase activity in patients with Parkinson's disease, with knowledge of the abundance of this enzyme in an individual, could personalize and potentially improve L-dopa therapies. In contrast, L-dopa decarboxylation by E.faecalis is not inhibited by carbidopa, a commonly used human L-dopa decarboxylase inhibitor.1 Publication

<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

kcat is 63.6 sec(-1) for the decarboxylation of L-tyrosine. kcat is 55.5 sec(-1) for the decarboxylation of L-dopa (at pH 5.5).1 Publication
  1. KM=315 µM for L-tyrosine (at pH 5.5)
  2. KM=1475 µM for L-dopa (at pH 5.5)

    pH dependencei

    L-dopa decarboxylation occurs more rapidly at lower pH, suggesting that this metabolism is likely accelerated at the lower pH of the upper small intestine.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Amino-acid metabolism

    This protein is involved in Amino-acid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in Amino-acid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei298Pyridoxal phosphateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei420Proton donorBy similarity1
    Binding sitei440Pyridoxal phosphate; shared with dimeric partnerBy similarity1

    <p>The <a href="http://www.geneontology.org/">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="http://www.uniprot.org/keywords">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 functionDecarboxylase, Lyase
    LigandPyridoxal phosphate

    <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="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
    L-tyrosine decarboxylase1 Publication (EC:4.1.1.251 Publication)
    Short name:
    TDC
    Short name:
    TyrDC1 Publication
    Alternative name(s):
    Levodopa decarboxylase1 Publication (EC:4.1.1.-1 Publication)
    Short name:
    L-dopa decarboxylase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:tyrDC1 Publication
    ORF Names:EFMMH594_12992Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEnterococcus faecalis (strain EnGen0310 / MMH594)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1158653 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene lose the ability to decarboxylate L-dopa, and display no growth defects compared with wild type.1 Publication

    <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_00004484981 – 620L-tyrosine decarboxylaseAdd BLAST620

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei392N6-(pyridoxal phosphate)lysineBy similarity1

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    By similarity

    <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

    More...
    SMRi
    P0DTQ4

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    Region

    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>Regioni158 – 159Pyridoxal phosphate bindingBy similarity2
    Regioni389 – 391Pyridoxal phosphate bindingBy similarity3

    <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

    More...
    Gene3Di
    3.40.640.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002129, PyrdxlP-dep_de-COase
    IPR015424, PyrdxlP-dep_Trfase
    IPR015421, PyrdxlP-dep_Trfase_major
    IPR022397, Tyrosine_deCO2ase_bac

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00282, Pyridoxal_deC, 2 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53383, SSF53383, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03811, tyr_de_CO2_Ent, 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="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">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="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P0DTQ4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKNEKLAKGE MNLNALFIGD KAENGQLYKD LLIDLVDEHL GWRQNYMPQD
    60 70 80 90 100
    MPVISSQERT SESYEKTVNH MKDVLNEISS RMRTHSVPWH TAGRYWGHMN
    110 120 130 140 150
    SETLMPSLLA YNFAMLWNGN NVAYESSPAT SQMEEEVGHE FAHLMSYKNG
    160 170 180 190 200
    WGHIVADGSL ANLEGLWYAR NIKSLPFAMK EVKPELVAGK SDWELLNMPT
    210 220 230 240 250
    KEIMDLLESA EDEIDEIKAH SARSGKHLQA IGKWLVPQTK HYSWLKAADI
    260 270 280 290 300
    IGIGLDQVIP VPVDHNYRMD INELEKIVRG LAEEQIPVLG VVGVVGSTEE
    310 320 330 340 350
    GAVDSIDKII ALRDELMKDG IYYYVHVDAA YGGYGRAIFL DEDNNFIPYE
    360 370 380 390 400
    DLQDVHEEYG VFKEKKEHIS REVYDAYKAI ELAESVTIDP HKMGYIPYSA
    410 420 430 440 450
    GGIVIQDIRM RDVISYFATY VFEKGADIPA LLGAYILEGS KAGATAASVW
    460 470 480 490 500
    AAHHVLPLNV AGYGKLIGAS IEGSHHFYNF LNDLTFKVGD KEIEVHTLTH
    510 520 530 540 550
    PDFNMVDYVF KEKGNDDLVA MNKLNHDVYD YASYVKGNIY NNEFITSHTD
    560 570 580 590 600
    FAIPDYGNSP LKFVNSLGFS DEEWNRAGKV TVLRAAVMTP YMNDKEEFDV
    610 620
    YAPKIQAALQ EKLEQIYDVK
    Length:620
    Mass (Da):70,053
    Last modified:November 13, 2019 - 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="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA83C598048C7D5E1
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AOPW01000049 Genomic DNA Translation: KKA47138.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_002355450.1, NZ_AOPW01000049.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    60892923

    <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="http://www.uniprot.org/help/uniref">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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AOPW01000049 Genomic DNA Translation: KKA47138.1
    RefSeqiWP_002355450.1, NZ_AOPW01000049.1

    3D structure databases

    SMRiP0DTQ4
    ModBaseiSearch...

    Genome annotation databases

    GeneIDi60892923

    Family and domain databases

    Gene3Di3.40.640.10, 1 hit
    InterProiView protein in InterPro
    IPR002129, PyrdxlP-dep_de-COase
    IPR015424, PyrdxlP-dep_Trfase
    IPR015421, PyrdxlP-dep_Trfase_major
    IPR022397, Tyrosine_deCO2ase_bac
    PfamiView protein in Pfam
    PF00282, Pyridoxal_deC, 2 hits
    SUPFAMiSSF53383, SSF53383, 1 hit
    TIGRFAMsiTIGR03811, tyr_de_CO2_Ent, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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 nameiTYRDC_ENTF3
    <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: P0DTQ4
    <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="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2019
    Last sequence update: November 13, 2019
    Last modified: June 2, 2021
    This is version 8 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 programProkaryotic 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

    Documents

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