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    panD aspartate 1-decarboxylase proenzyme [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945686, updated on 3-Dec-2024

    Summary

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    Official Symbol
    panD
    Official Full Name
    aspartate 1-decarboxylase proenzyme
    Primary source
    ECOCYC:EG11747
    Locus tag
    b0131
    See related
    ASAP:ABE-0000459
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK0130
    Summary
    Mutants have altered acyl-CoA pools. [More information is available at EcoGene: EG11747]. The subunit of aspartate 1-decarboxylase is the smaller N-terminal cleavage product of PanD . [More information is available at EcoCyc: EG11747].
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    Genomic context

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    Sequence:
    NC_000913.3 (146314..146694, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative PTS enzyme IIA component YadI Neighboring gene putative polysaccharide deacetylase lipoprotein YadE Neighboring gene recombination-promoting nuclease RpnC Neighboring gene pantothenate synthetase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Breaking up is easy with esters. Perler FB. Nat Struct Biol, 1998 Apr. PMID 9546209
    2. Purification and properties of L-Aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli. Williamson JM, et al. J Biol Chem, 1979 Aug 25. PMID 381298
    3. Alkylation of an active-site cysteinyl residue during substrate-dependent inactivation of Escherichia coli S-adenosylmethionine decarboxylase. Diaz E, et al. Biochemistry, 1991 Apr 23. PMID 2018773
    4. Pyruvoyl-dependent enzymes. van Poelje PD, et al. Annu Rev Biochem, 1990. PMID 2197977
    5. Beta-alanine synthesis in Escherichia coli. Cronan JE Jr. J Bacteriol, 1980 Mar. PMID 6767707, Free PMC Article

    See all (22) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Most vitamin biosynthetic pathways in bacteria are tightly regulated. Data suggest binding of panZ/AcCoA complex to panD regulates pantothenate biosynthesis; this multimerization leads to sequestration of pyruvoyl cofactor as ketone hydrate and activation of panD; antimetabolite N-pentyl-pantothenamide inhibits panD. (panD = aspartate-alpha-decarboxylase; panZ = panD autocleavage accelerator; AcCoA = acetyl coenzyme A)
      Title: The Mechanism of Regulation of Pantothenate Biosynthesis by the PanD-PanZ·AcCoA Complex Reveals an Additional Mode of Action for the Antimetabolite N-Pentyl Pantothenamide (N5-Pan).
    2. N-terminus verified by Edman degradation on complete protein
      Title: Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables aspartate 1-decarboxylase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables aspartate 1-decarboxylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables carboxy-lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in alanine biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in alanine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in pantothenate biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in pantothenate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein autoprocessing IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    aspartate 1-decarboxylase proenzyme
    NP_414673.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      146314..146694 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414673.1 aspartate 1-decarboxylase proenzyme [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414673.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7EBM2
      Conserved Domains (1) summary
      TIGR00223
      Location:1 → 126
      panD; L-aspartate-alpha-decarboxylase
    Nucleotide Protein
    Heading Accession and Version

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