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nadB L-aspartate oxidase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947049, updated on 4-Apr-2024

Summary

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Gene symbol
nadB
Gene description
L-aspartate oxidase
Primary source
ASAP:ABE-0008471
Locus tag
b2574
See related
ECOCYC:EG10631
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
ECK2572; nic; nicB
Summary
L-aspartate oxidase (NadB) is the first enzyme in the de novo NAD biosynthesis pathway, catalyzing the FAD-dependent oxidation of L-aspartate to iminoaspartate . [More information is available at EcoCyc: EG10631].
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Genomic context

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Sequence:
NC_000913.3 (2710420..2712042)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene anti-sigma factor stabilizing protein RseB Neighboring gene anti-sigma-E factor RseA Neighboring gene RNA polymerase sigma factor RpoE Neighboring gene rpoE leader peptide Neighboring gene tRNA m(6)A37 methyltransferase Neighboring gene ATP-dependent RNA helicase SrmB Neighboring gene putative LysR-type DNA-binding transcriptional regulator YfiE

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. Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis. Bossi RT, et al. Biochemistry, 2002 Mar 5. PMID 11863440
  2. Probing the active site of L-aspartate oxidase by site-directed mutagenesis: role of basic residues in fumarate reduction. Tedeschi G, et al. Biochemistry, 2001 Apr 17. PMID 11294641
  3. Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis. Tedeschi G, et al. Eur J Biochem, 1999 Mar. PMID 10103021
  4. Redox potentials and quinone reductase activity of L-aspartate oxidase from Escherichia coli. Tedeschi G, et al. Biochemistry, 1997 Dec 23. PMID 9405056
  5. L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity. Tedeschi G, et al. Eur J Biochem, 1996 Jul 15. PMID 8706750

See all (30) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. N-terminus verified by Edman degradation on complete protein
    Title: Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB.
Submit: New GeneRIF Correction

Pathways from PubChem

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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 L-aspartate oxidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables L-aspartate oxidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables L-aspartate oxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables L-aspartate oxidase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables L-aspartate:fumarate oxidoreductase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables L-aspartate:fumarate oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables flavin adenine dinucleotide binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in 'de novo' NAD biosynthetic process from aspartate IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within 'de novo' NAD biosynthetic process from aspartate IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in NAD biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in pyridine nucleotide biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
L-aspartate oxidase
NP_417069.1

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
    2710420..2712042
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417069.1 L-aspartate oxidase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417069.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A827XUM0, U5NVE5
    Conserved Domains (1) summary
    PRK09077
    Location:1 → 537
    PRK09077; L-aspartate oxidase; Provisional
Nucleotide Protein
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