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Evolutionarily divergent DUF4465 domains have a common vitamin B12-binding function.

Charlea Clarke1, Michal Banasik1, Rokas Juodeikis2

  • 1School of Biological and Behavioural Sciences, Queen Mary University of London, UK.

FEBS Open Bio
|March 18, 2026
PubMed
Summary

The DUF4465 protein family, found across diverse bacteria, commonly binds vitamin B12. This function is crucial for bacterial survival, especially in environments with limited B12 availability.

Keywords:
B12‐binding proteinsB12‐scavenging proteinsDUF4465 (DUF Domain of Unknown Function)IPR027828 family proteinsmicrobiomeβ‐jellyroll proteins

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The DUF4465 protein family comprises over 1000 members found in diverse bacterial species and environments.
  • In *Bacteroides thetaiotaomicron*, DUF4465 proteins are essential for scavenging vitamin B12 (cobalamin), a vital cofactor for bacteria unable to synthesize it.
  • The prevalence of B12-binding across the DUF4465 family remained largely uncharacterized.

Purpose of the Study:

  • To investigate the functional conservation of B12-binding within the DUF4465 protein family.
  • To determine if B12-binding is a ubiquitous or recurrent function across diverse DUF4465 members.
  • To establish the structural and functional significance of DUF4465 proteins in microbial B12 acquisition.

Main Methods:

  • Bioinformatic analysis of DUF4465 family distribution and sequence conservation.
  • Experimental characterization of B12-binding activity in selected DUF4465 family members.
  • Structural analysis of DUF4465 proteins to identify conserved B12-binding motifs.

Main Results:

  • B12-binding was confirmed as a recurrent function in eight distantly related DUF4465 family members.
  • The DUF4465 domain defines a structurally conserved, augmented β-jellyroll fold adept at binding cobalamin.
  • These findings suggest B12-binding is a common functional trait for the majority of DUF4465 proteins.

Conclusions:

  • DUF4465 proteins represent a widespread and structurally conserved family of bacterial B12-binding proteins.
  • This family plays significant roles in microbial competition for the essential cofactor, vitamin B12.
  • The DUF4465 domain serves as a promising scaffold for developing protein-based B12 capture and purification technologies.