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 [3,4].
Staphylococci signal transduction protein TRAP (target of RNAIII-
activating protein) .
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 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 βαβ-fold with an antiparallel β-sheet (see <1IUJ>). 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 [1,2,3,5,7,8].
The profile we developed covers the entire ABM domain.
July 2014 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Sciara G. Kendrew S.G. Miele A.E. Marsh N.G. Federici L. Malatesta F. Schimperna G. Savino C. Vallone B.
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.
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