U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    pabB aminodeoxychorismate synthase subunit 1 [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946337, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    pabB
    Official Full Name
    aminodeoxychorismate synthase subunit 1
    Primary source
    ECOCYC:EG10683
    Locus tag
    b1812
    See related
    ASAP:ABE-0006031
    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
    ECK1810
    Summary
    Component I catalyzes the formation of ADC by binding chorismate and ammonia. [More information is available at EcoCyc: EG10683].
    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 (1894805..1896166)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF1889 domain-containing protein YoaC Neighboring gene UFP0181 family protein YoaH Neighboring gene putative NUDIX hydrolase with low 3-phosphohydroxypyruvate phosphatase activity Neighboring gene L-serine deaminase I

    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. Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes. Parsons JF, et al. Biochemistry, 2002 Feb 19. PMID 11841211
    2. p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA. Roux B, et al. Biochemistry, 1993 Apr 13. PMID 8096767
    3. p-aminobenzoate synthesis in Escherichia coli: kinetic and mechanistic characterization of the amidotransferase PabA. Roux B, et al. Biochemistry, 1992 Aug 4. PMID 1637823
    4. Chorismate aminations: partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase. Walsh CT, et al. Biochemistry, 1987 Jul 28. PMID 3311153
    5. Genetic analysis of mutant strains of Escherichia coli requiring p-aminobenzoic acid for growth. Huang M, et al. J Bacteriol, 1967 Jun. PMID 5337773, Free PMC Article

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 4-amino-4-deoxychorismate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 4-amino-4-deoxychorismate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 4-amino-4-deoxychorismate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein heterodimerization activity IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tryptophan binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in folic acid biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in folic acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in folic acid-containing compound biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within para-aminobenzoic acid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tetrahydrofolate biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tetrahydrofolate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tryptophan biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    part_of aminodeoxychorismate synthase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of aminodeoxychorismate synthase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    aminodeoxychorismate synthase subunit 1
    NP_416326.1

    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
      1894805..1896166
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416326.1 aminodeoxychorismate synthase subunit 1 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416326.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8T6BHI9
      Conserved Domains (1) summary
      PRK15465
      Location:1 → 453
      pabB; aminodeoxychorismate synthase component 1
    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.