| Description | 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 [ ].Escherichia coli probable quinol monooxygenase YgiN, can oxidize menadiol to menadione [ ].Staphylococcus aureus heme-degrading enzymes IsdG and IsdI [ , ].Staphylococci signal transduction protein TRAP (target of RNAIII- activating protein) [ ].Mycobacterium tuberculosis heme-degrading monooxygenase MhuD (or Rv3592) [ ].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 [ ].Thermus thermophilus hypothetical protein TT1380 [ ].The ABM domain has only moderate sequence homology while sharing a high degree of structural similarity. The ABM domain crystallises as a homodimer. Each monomer is composed of three α-helices (H1-3) and four β-strands (S1-4) and has a ferredoxin-like split β-α-β-fold with an antiparallel β-sheet [ ]. The β-sheets of two monomers form a 10-strand, anti- parallel β-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 [, , , , , ]. | Name | Antibiotic biosynthesis monooxygenase domain |
| Short Name | ABM_dom | Type | Domain |
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