| Type: | Domain | Name: | Antibiotic biosynthesis monooxygenase domain |
| 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 antibioticactinorhodin, 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 scavengerthat 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 crystallizes as a homodimer. Eachmonomer 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 []. 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 theother providing important interactions within the dimer. The core of the barrel is mainly hydrophobic [, , , , , ]. | Short Name: | ABM_dom |
