acoL

168

acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)

Locus: BSU_08090

Molecular weight: 48.69 kDa

Isoelectric point: 5.27

Protein length: 458 aa

Gene length: 1377 bp

Function: acetoin utilization

Product: acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)

Essential: no

E.C.: 1.8.1.4

Synonyms: acoL, yfjH

Genomic Context

Hide small RNAsZoom:

List of homologs in different organisms, belongs to COG1249 (Galperin et al., 2021)

Gene

Coordinates: 882,266  883,642

The protein

Catalyzed reaction/ biological activity

• Protein N⁶-(dihydrolipoyl)lysine + NAD⁺ --> protein N⁶-(lipoyl)lysine + NADH (according to UniProt)

Protein family

• class-I pyridine nucleotide-disulfide oxidoreductase family (with PdhD and LpdV, according to UniProt)

Cofactors

• FAD (according to UniProt)

Structure

• 2EQ7 (PDB) (from Thermus thermophilus, 40% identity)
• O34324 (AlphaFold)

Paralogous protein(s)

• PdhD, LpdV

Localization

• cytoplasm (according to UniProt)

Expression and Regulation

Operons

• Genes: acoA-acoB-acoC-acoL

  Description: PubMed

  Regulation

  • induced by acetoin (AcoR) PubMed

  Regulatory mechanism

  • CcpA: repression, PubMed, in ccpA regulon
  • AcoR: activation, (interaction with SigL-containing RNA polymerase) [ PubMed|11274109], in acoR regulon
  • Fnr: indirect positive regulation, in fnr regulon

  Sigma factors

  • SigL: sigma factor, PubMed, in sigL regulon

  Additional information

  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Additional information

• the mRNA is very stable (> 15 min) PubMed

Biological materials

Mutant

• MGNA-C351 (acoL::erm), available at the NBRP B. subtilis, Japan
• BKE08090 (acoL::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATGTCGTTTTCACCTGCTT,  downstream forward: _UP4_TAATAAAGGAAAAAGCAGGC
• BKK08090 (acoL::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATGTCGTTTTCACCTGCTT,  downstream forward: _UP4_TAATAAAGGAAAAAGCAGGC

Two-hybrid system

• B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

Labs working on this gene/protein

• Michel Debarbouille, Pasteur Institute, Paris, France Homepage

References

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