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

Gene ID: 945686, updated on 23-Nov-2023

Summary

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Gene symbol
panD
Gene description
aspartate 1-decarboxylase proenzyme
Primary source
ASAP:ABE-0000459
Locus tag
b0131
See related
ECOCYC:EG11747
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. Tools for metabolic engineering in Escherichia coli: inactivation of panD by a point mutation. Kennedy J, et al. Anal Biochem, 2004 Apr 1. PMID 15033515
  2. Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase. Schmitzberger F, et al. EMBO J, 2003 Dec 1. PMID 14633979, Free PMC Article
  3. Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction. Saldanha SA, et al. Chem Commun (Camb), 2001 Sep 21. PMID 12240302
  4. Breaking up is easy with esters. Perler FB. Nat Struct Biol, 1998 Apr. PMID 9546209
  5. Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry. Ramjee MK, et al. Biochem J, 1997 May 1. PMID 9169598, Free PMC Article

See all (23) 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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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
  
enables 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
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