Pathways & interactions
Antibiotic biosynthesis monooxygenase domain (IPR007138)
Short name: ABM_dom
Overlapping homologous superfamilies
- Dimeric alpha-beta barrel (IPR011008)
The antibiotic biosynthesis monooxygenase (ABM) domain is found in proteins involved in a diverse range of biological processes, including metabolism, transcription, translation and biosynthesis of secondary metabolites:
- Streptomyces coelicolor ActVA-Orf6 monooxygenase, plays a role in the biosynthesis of aromatic polyketides, specifically the antibiotic actinorhodin, by oxidizing phenolic groups to quinones [PMID: 12514126].
- Escherichia coli probable quinol monooxygenase YgiN, can oxidize menadiol to menadione [PMID: 15613473].
- Staphylococcus aureus heme-degrading enzymes IsdG and IsdI [PMID: 15520015, PMID: 18713745].
- Staphylococci signal transduction protein TRAP (target of RNAIII- activating protein) [PMID: 22750855].
- Mycobacterium tuberculosis heme-degrading monooxygenase MhuD (or Rv3592) [PMID: 19917297].
- Mycobacterium tuberculosis putative monooxygenase Rv0793, might be involved in antibiotic biosynthesis, or may act as reactive oxygen species scavenger that could help in evading host defenses [PMID: 16496224].
- Thermus thermophilus hypothetical protein TT1380 [PMID: 15103643].
The ABM domain has only moderate sequence homology while sharing a high degree of structural similarity. The ABM domain crystallizes as a homodimer. Each monomer is composed of three alpha-helices (H1-3) and four beta-strands (S1-4) and has a ferredoxin-like split BetaAlphaBeta-fold with an antiparallel beta- sheet [PMID: 15103643]. The beta-sheets of two monomers form a 10-strand, anti- parallel beta-barrel. The barrel is built of two smaller sheets that are connected by long C-terminal strands crossing over from one monomer to the other providing important interactions within the dimer. The core of the barrel is mainly hydrophobic [PMID: 12514126, PMID: 15613473, PMID: 15520015, PMID: 22750855, PMID: 16496224, PMID: 15103643].