U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

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

Gene ID: 947049, updated on 17-Dec-2024

Summary

Go to the top of the page Help
Official Symbol
nadB
Official Full Name
L-aspartate oxidase
Primary source
ECOCYC:EG10631
Locus tag
b2574
See related
ASAP:ABE-0008471
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].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
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

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase. Seifert J, et al. Biol Chem Hoppe Seyler, 1990 Mar. PMID 2187483
  2. L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. Nasu S, et al. J Biol Chem, 1982 Jan 25. PMID 7033218
  3. L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Mortarino M, et al. Eur J Biochem, 1996 Jul 15. PMID 8706749
  4. Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis. Bossi RT, et al. Biochemistry, 2002 Mar 5. PMID 11863440
  5. 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

See all (29) 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

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

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 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

Go to the top of the page Help
Preferred Names
L-aspartate oxidase
NP_417069.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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
    U5NVE5
    Conserved Domains (1) summary
    PRK09077
    Location:1 → 537
    PRK09077; L-aspartate oxidase; Provisional
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.