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citE citrate lyase beta subunit [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945406, updated on 6-Jul-2026
Official Symbol
citE
Official Full Name
citrate lyase beta subunit
Primary source
ECOCYC:G6342
Locus tag
b0616
See related
ASAP:ABE-0002122
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0609; ybdW
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Try the new Transcripts and proteins table
Sequence:
NC_000913.3 (649582..650490, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene triphosphoribosyl-dephospho-CoA synthase Neighboring gene apo-citrate lyase phosphoribosyl-dephospho-CoA transferase Neighboring gene citrate lyase alpha subunit Neighboring gene citrate lyase acyl carrier protein Neighboring gene citrate lyase synthetase Neighboring gene sensor histidine kinase DpiB Neighboring gene DNA-binding transcriptional dual regulator DpiA

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Reevaluation of citrate lyase from Escherichia coli. Quentmeier A, et al. Biochim Biophys Acta, 1987 May 27. PMID 3555623
  2. CORRELATION OF CITRATE UTILIZATION BY MEMBERS OF THE COLON-AEROGENES GROUP WITH OTHER DIFFERENTIAL CHARACTERISTICS AND WITH HABITAT. Koser SA. J Bacteriol, 1924 Jan. PMID 16559027, Free PMC Article
  3. Why a co-substrate is required for anaerobic growth of Escherichia coli on citrate. Lütgens M, et al. J Gen Microbiol, 1980 Jul. PMID 6997437
  4. SOS response induction by beta-lactams and bacterial defense against antibiotic lethality. Miller C, et al. Science, 2004 Sep 10. PMID 15308764
  5. The binary protein-protein interaction landscape of Escherichia coli. Rajagopala SV, et al. Nat Biotechnol, 2014 Mar. PMID 24561554, Free PMC Article

See all (8) citations in PubMed

GeneRIFs: Gene References Into Functions

Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables citrate (pro-3S)-lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables citryl-CoA lyase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in acetyl-CoA metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in acetyl-CoA metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in citrate metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in citrate metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in oxaloacetate metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
part_of ATP-independent citrate lyase complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of ATP-independent citrate lyase complex IEA
Inferred from Electronic Annotation
more info
  
part_of ATP-independent citrate lyase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
citrate lyase beta subunit
NP_415149.4

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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
    649582..650490 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415149.4 citrate lyase beta subunit

    See identical proteins and their annotated locations for NP_415149.4

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A0H2YXI8
    Conserved Domains (1) summary
    cl21481
    Location:12 → 299
    malate_synt; Malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms, like plants and fungi, to derive their ...
Nucleotide Protein
Heading Accession and Version

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