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Entry version 29 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Aspartate 1-decarboxylase



Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.UniRule annotation1 Publication
Overexpression of wild-type protein confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA).1 Publication


Pantothenate, pantetheine and beta-alanine containing compounds (all part of the panthothenate/coenzyme A biosynthetic pathway) antagonize PZA and POA antitubercular activity. However cultivation of the double panD and panC mutant with low levels of pantetheine (an intermediate between pantothenate and coenzyme A, at pH 5.8) restores sensitivity to PZA, suggesting PanD is not the PZA target.1 Publication

<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

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

<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 0.65 sec(-1), specific activity 2100 nmol/min/mg for L-asparate.1 Publication
  1. KM=219.6 µM for L-aspartate1 Publication

    <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: (R)-pantothenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes beta-alanine from L-aspartate.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Aspartate 1-decarboxylase (panD)
    This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes beta-alanine from L-aspartate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">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 sitei25Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation1
    <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 sitei57SubstrateUniRule annotation1
    Active sitei58Proton donorUniRule annotation1

    <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

    • aspartate 1-decarboxylase activity Source: MTBBASE

    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 functionDecarboxylase, Lyase
    Biological processPantothenate biosynthesis, Virulence
    LigandPyruvate, Schiff base

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases


    UniPathway: a resource for the exploration and annotation of metabolic pathways


    <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:
    Aspartate 1-decarboxylaseUniRule annotation (EC: annotation1 Publication)
    Alternative name(s):
    Aspartate alpha-decarboxylaseUniRule annotation
    Cleaved into the following 2 chains:
    Aspartate 1-decarboxylase beta chainUniRule annotation
    Aspartate 1-decarboxylase alpha chainUniRule annotation
    <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:panDUniRule annotation
    Ordered Locus Names:Rv3601c
    ORF Names:MTCY07H7B.21
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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: Chromosome

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database


    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti


    <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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Subcutaneous immunization with the double panD and panC bacterial disruption mutant protects mice for over a year against subsequent virulent M.tuberculosis (strain Erdman) infections; mice show mild lung inflammation and fibrosis despite a chronic bacterila infection. This is a promising attenuated vaccine strain.1 Publication

    <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

    Simultaneous disruption of panD and panC gives a mutant unable to grow in the absence of panothenate. The double mutant has a highly attenuated disease response in BALB/c and SCID mice; immunocompromised BALB/c SCID mice survive on average 36 weeks as opposed to 5 weeks for mice infected with wild-type bacteria, while immunocompetent BALB/c mice survive indefinitely. In wild-type mice bacteria grow for 3 weeks then undergo a steady decline, bacteria persist over 8 months in SCID mice (PubMed:12219086). The double mutant is sensitive to PZA but not POA in liquid culture, beta-alanine but not pantothenate antagonize the effect of PZA at pH 5.8 (PubMed:25246400).2 Publications


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi21H → R in S11; may confer PZA resistance; when associated with V-49. 1 Publication1
    Mutagenesisi49I → V in S11; may confer PZA resistance; when associated with R-21. 1 Publication1
    Mutagenesisi128A → S in S6; may confer PZA resistance. 1 Publication1
    Mutagenesisi130E → G in S13; may confer PZA resistance. 1 Publication1
    Mutagenesisi138V → A in S9, S10; may confer PZA resistance. 1 Publication1

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000231211 – 24Aspartate 1-decarboxylase beta chainUniRule annotation1 PublicationAdd BLAST24
    ChainiPRO_000002312225 – 139Aspartate 1-decarboxylase alpha chainUniRule annotation1 PublicationAdd BLAST115

    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="">lipids</a>, <a href="">glycans</a> and <a href="">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25Pyruvic acid (Ser)UniRule annotation1

    <p>This subsection of the <a href="">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. Cleavage is not necessary for tetramerization upon expression in E.coli; protein expressed in E.coli is fully process in vitro after 48 hours at 37 degrees Celsius (PubMed:12182836).UniRule annotation1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Zymogen

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life


    <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="">'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="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Heterooctamer of four alpha and four beta subunits.

    UniRule annotation1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks


    <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

    Secondary structure

    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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


    Database of comparative protein structure models


    Protein Data Bank in Europe - Knowledge Base


    <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>Regioni73 – 75Substrate bindingUniRule annotation3

    <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

    Belongs to the PanD family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    ENOG4108Z2X Bacteria
    COG0853 LUCA

    KEGG Orthology (KO)


    Identification of Orthologs from Complete Genome Data


    Database for complete collections of gene phylogenies


    Family and domain databases

    Conserved Domains Database

    cd06919 Asp_decarbox, 1 hit

    HAMAP database of protein families

    MF_00446 PanD, 1 hit

    Integrated resource of protein families, domains and functional sites

    View protein in InterPro
    IPR009010 Asp_de-COase-like_dom_sf
    IPR003190 Asp_decarbox

    The PANTHER Classification System

    PTHR21012 PTHR21012, 1 hit

    Pfam protein domain database

    View protein in Pfam
    PF02261 Asp_decarbox, 1 hit

    PIRSF; a whole-protein classification database

    PIRSF006246 Asp_decarbox, 1 hit

    Superfamily database of structural and functional annotation

    SSF50692 SSF50692, 1 hit

    TIGRFAMs; a protein family database

    TIGR00223 panD, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P9WIL3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    60 70 80 90 100
    110 120 130
    Mass (Da):14,885
    Last modified:April 16, 2014 - 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:iC5BFDC1C996ED9C6

    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
    AL123456 Genomic DNA Translation: CCP46424.1

    Protein sequence database of the Protein Information Resource


    NCBI Reference Sequences

    NP_218118.1, NC_000962.3
    WP_003419523.1, NZ_NVQJ01000056.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    CCP46424; CCP46424; Rv3601c

    Database of genes from NCBI RefSeq genomes


    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
    AL123456 Genomic DNA Translation: CCP46424.1
    RefSeqiNP_218118.1, NC_000962.3
    WP_003419523.1, NZ_NVQJ01000056.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe


    Protein Data Bank RCSB


    Protein Data Bank Japan

    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum

    Protein-protein interaction databases


    Proteomic databases


    Genome annotation databases

    EnsemblBacteriaiCCP46424; CCP46424; Rv3601c

    Organism-specific databases


    Phylogenomic databases

    eggNOGiENOG4108Z2X Bacteria
    COG0853 LUCA

    Enzyme and pathway databases


    Family and domain databases

    CDDicd06919 Asp_decarbox, 1 hit
    HAMAPiMF_00446 PanD, 1 hit
    InterProiView protein in InterPro
    IPR009010 Asp_de-COase-like_dom_sf
    IPR003190 Asp_decarbox
    PANTHERiPTHR21012 PTHR21012, 1 hit
    PfamiView protein in Pfam
    PF02261 Asp_decarbox, 1 hit
    PIRSFiPIRSF006246 Asp_decarbox, 1 hit
    SUPFAMiSSF50692 SSF50692, 1 hit
    TIGRFAMsiTIGR00223 panD, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins


    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 nameiPAND_MYCTU
    <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: P9WIL3
    Secondary accession number(s): L0TDA1, O06281, P65660
    <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: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: October 16, 2019
    This is version 29 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome


    1. SIMILARITY comments
      Index of protein domains and families
    2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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