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nanA N-acetylneuraminate lyase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947742, updated on 3-Dec-2024
Official Symbol
nanA
Official Full Name
N-acetylneuraminate lyase
Primary source
ECOCYC:EG10637
Locus tag
b3225
See related
ASAP:ABE-0010579
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
ECK3214
Summary
N-acetylneuraminate lyase is the first enzyme in the pathway for degradation of sialic acid (N-acetylneuraminate, or NeuNAc) . [More information is available at EcoCyc: EG10637].
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Sequence:
NC_000913.3 (3372683..3373576, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene N-acetylmannosamine kinase Neighboring gene putative N-acetylmannosamine-6-phosphate 2-epimerase Neighboring gene N-acetylneuraminate:H(+) symporter Neighboring gene NanR Neighboring gene putative transporter DcuD

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251. Chou CY, et al. J Biol Chem, 2011 Apr 22. PMID 21270125, Free PMC Article
  2. High-level production and purification of Escherichia coli N-acetylneuraminic acid aldolase (EC 4.1.3.3). Lilley GG, et al. Protein Expr Purif, 1992 Oct. PMID 1458058
  3. Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli. Aisaka K, et al. Biochem J, 1991 Jun 1. PMID 1646603, Free PMC Article
  4. Inhibition of N-acetylneuraminate lyase by N-acetyl-4-oxo-D-neuraminic acid. Gross HJ, et al. FEBS Lett, 1988 May 9. PMID 2896604
  5. Genetic and molecular analyses of Escherichia coli N-acetylneuraminate lyase gene. Kawakami B, et al. J Bacteriol, 1986 Jul. PMID 3522555, Free PMC Article

See all (31) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. analysis of modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251
    Title: Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251.
  2. A comparison of mutant and wild-type nanA structures, in combination with the specificity profiles of the variants, reveals subtle differences that explain the details of the substrate specificity changes.
    Title: Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
  3. Results describe the structure of a mutant variant of Escherichia coli N-acetyl-d-neuraminic acid lyase (NAL), E192N, in complex with pyruvate in a new crystal form.
    Title: Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution.
  4. the dimer-dimer interface of NAL is intolerant to mutation and essential for functional expression.
    Title: The quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression.
  5. N-terminus verified by Edman degradation on complete protein
    Title: Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables N-acetylneuraminate lyase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables N-acetylneuraminate lyase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables N-acetylneuraminate lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in N-acetylneuraminate catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in N-acetylneuraminate catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in N-acetylneuraminate catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in carbohydrate metabolic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within_positive_effect single-species biofilm formation IMP
Inferred from Mutant Phenotype
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 
Preferred Names
N-acetylneuraminate lyase

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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
    3372683..3373576 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417692.1 N-acetylneuraminate lyase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417692.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376JRE7, A0A5B9ANI8, A0A7D7EZH8
    Conserved Domains (1) summary
    TIGR00683
    Location:5 → 297
    nanA; N-acetylneuraminate lyase
Nucleotide Protein
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