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    abgA p-aminobenzoyl-glutamate hydrolase subunit A [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945742, updated on 3-Dec-2024

    Summary

    Official Symbol
    abgA
    Official Full Name
    p-aminobenzoyl-glutamate hydrolase subunit A
    Primary source
    ECOCYC:G6670
    Locus tag
    b1338
    See related
    ASAP:ABE-0004493
    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
    ECK1334; ydaJ
    Summary
    abgAB expression is required for catabolism to feed p-aminobenzoate auxotrophs (Hussein, 1998; Carter, 2007). [More information is available at EcoGene: EG13352]. AbgA has similarity to aminoacyl aminohydrolases . [More information is available at EcoCyc: G6670].
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    Genomic context

    Sequence:
    NC_000913.3 (1403255..1404565, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene methylated-DNA--[protein]-cysteine S-methyltransferase Neighboring gene p-aminobenzoyl glutamate:H(+) symporter Neighboring gene p-aminobenzoyl-glutamate hydrolase subunit B Neighboring gene putative LysR-type DNA-binding transcriptional regulator AbgR Neighboring gene ncRNA

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables dipeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds IEA
    Inferred from Electronic Annotation
    more info
     
    enables para-aminobenzoyl-glutamate hydrolase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables para-aminobenzoyl-glutamate hydrolase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables para-aminobenzoyl-glutamate hydrolase activity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    enables protein heterodimerization activity IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in folic acid catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in folic acid catabolic process IDA
    Inferred from Direct Assay
    more info
    PubMed 
    acts_upstream_of_or_within folic acid catabolic process IGI
    Inferred from Genetic Interaction
    more info
    PubMed 
    Component Evidence Code Pubs
    part_of catalytic complex IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    PubMed 

    General protein information

    Preferred Names
    p-aminobenzoyl-glutamate hydrolase subunit A

    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
      1403255..1404565 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415854.4 p-aminobenzoyl-glutamate hydrolase subunit A [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415854.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1KT43, A0A376K160
      Conserved Domains (1) summary
      cd05665
      Location:13428
      M20_Acy1_IAAspH; M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase