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entF apo-serine activating enzyme [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945184, updated on 10-Oct-2024

Summary

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Official Symbol
entF
Official Full Name
apo-serine activating enzyme
Primary source
ECOCYC:EG10264
Locus tag
b0586
See related
ASAP:ABE-0002021
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
ECK0579
Summary
Apo-serine activating enzyme is phosphopantetheinylated posttranslationally resulting in the active enzyme form, serine activating enzyme. [More information is available at EcoCyc: EG10264].
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Genomic context

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Sequence:
NC_000913.3 (614157..618038)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ferric enterobactin outer membrane transporter Neighboring gene ferric enterobactin esterase Neighboring gene enterobactin biosynthesis protein YbdZ Neighboring gene polysaccharide co-polymerase family protein FepE Neighboring gene ferric enterobactin ABC transporter ATP binding subunit Neighboring gene ferric enterobactin ABC transporter membrane subunit FepG Neighboring gene ferric enterobactin ABC transporter membrane subunit FebD

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. Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase. Frueh DP, et al. Nature, 2008 Aug 14. PMID 18704088, Free PMC Article
  2. The production in vivo of microcin E492 with antibacterial activity depends on salmochelin and EntF. Mercado G, et al. J Bacteriol, 2008 Aug. PMID 18502859, Free PMC Article
  3. Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization. Shaw-Reid CA, et al. Chem Biol, 1999 Jun. PMID 10375542
  4. The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates. Ehmann DE, et al. Proc Natl Acad Sci U S A, 2000 Mar 14. PMID 10688898, Free PMC Article
  5. In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH. Chen D, et al. Biochemistry, 2009 Jan 27. PMID 19119850, Free PMC Article

See all (25) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. mutants in entF did not produce active microcin E492 in the presence of enterochelin or salmochelin.
    Title: The production in vivo of microcin E492 with antibacterial activity depends on salmochelin and EntF.
  2. N-terminus verified by Edman degradation on complete protein
    Title: Transcriptional mapping and nucleotide sequence of the Escherichia coli fepA-fes enterobactin region. Identification of a unique iron-regulated bidirectional promoter.
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 2,3-dihydroxybenzoate-serine ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 2,3-dihydroxybenzoate-serine ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 2,3-dihydroxybenzoate-serine ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables nucleotidyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphopantetheine binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables phosphopantetheine binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphopantetheine binding IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in amino acid activation for nonribosomal peptide biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within amino acid activation for nonribosomal peptide biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in enterobactin biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in enterobactin biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within enterobactin biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in secondary metabolite biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of enterobactin synthetase complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of enterobactin synthetase complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
apo-serine activating enzyme
NP_415118.1

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
    614157..618038
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415118.1 apo-serine activating enzyme [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415118.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8I0C9S3, A0AAN5J0U9
    Conserved Domains (1) summary
    PRK10252
    Location:1 → 1292
    entF; enterobactin non-ribosomal peptide synthetase EntF
Nucleotide Protein
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