Protein Domain : Antibiotic biosynthesis monooxygenase domain IPR007138

Type	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 degreeof structural similarity. The ABM domain crystallizes 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 BetaAlphaBeta-fold with an antiparallel beta- 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 theother providing important interactions within the dimer. The core of the barrel is mainly hydrophobic [, , , , , ].
Short Name	ABM_dom