PROSITE documentation PDOC51725
ABM domain profile


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 [1].
  • Escherichia coli probable quinol monooxygenase YgiN, can oxidize menadiol to menadione [2].
  • Staphylococcus aureus heme-degrading enzymes IsdG and IsdI [3,4].
  • Staphylococci signal transduction protein TRAP (target of RNAIII- activating protein) [5].
  • Mycobacterium tuberculosis heme-degrading monooxygenase MhuD (or Rv3592) [6].
  • 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 [7].
  • Thermus thermophilus hypothetical protein TT1380 [8].

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.

Last update:

July 2014 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ABM, PS51725; ABM domain profile  (MATRIX)


1AuthorsSciara G. Kendrew S.G. Miele A.E. Marsh N.G. Federici L. Malatesta F. Schimperna G. Savino C. Vallone B.
TitleThe structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.
SourceEMBO J. 22:205-215(2003).
PubMed ID12514126

2AuthorsAdams M.A. Jia Z.
TitleStructural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli: identification of a novel quinol monooxygenase.
SourceJ. Biol. Chem. 280:8358-8363(2005).
PubMed ID15613473

3AuthorsWu R. Skaar E.P. Zhang R. Joachimiak G. Gornicki P. Schneewind O. Joachimiak A.
TitleStaphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.
SourceJ. Biol. Chem. 280:2840-2846(2005).
PubMed ID15520015

4AuthorsLee W.C. Reniere M.L. Skaar E.P. Murphy M.E.P.
TitleRuffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus.
SourceJ. Biol. Chem. 283:30957-30963(2008).
PubMed ID18713745

5AuthorsHenrick K. Hirshberg M.
TitleStructure of the signal transduction protein TRAP (target of RNAIII-activating protein).
SourceActa Crystallogr. F 68:744-750(2012).
PubMed ID22750855

6AuthorsChim N. Iniguez A. Nguyen T.Q. Goulding C.W.
TitleUnusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis.
SourceJ. Mol. Biol. 395:595-608(2010).
PubMed ID19917297

7AuthorsLemieux M.J. Ference C. Cherney M.M. Wang M. Garen C. James M.N.G.
TitleThe crystal structure of Rv0793, a hypothetical monooxygenase from M. tuberculosis.
SourceJ. Struct. Funct. Genomics 6:245-257(2005).
PubMed ID16496224

8AuthorsWada T. Shirouzu M. Terada T. Kamewari Y. Park S.-Y. Tame J.R.H. Kuramitsu S. Yokoyama S.
TitleCrystal structure of the conserved hypothetical protein TT1380 from Thermus thermophilus HB8.
SourceProteins 55:778-780(2004).
PubMed ID15103643

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