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

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

    Summary

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    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].
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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. 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

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    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 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

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

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