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	PROSITE documentation PDOC51725

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.

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

ABM, PS51725; ABM domain profile  (MATRIX)

• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 119
  • detected by PS51725: 119 (true positives)
  • undetected by PS51725: 0 (false negative or 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51725:
  NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51725
  
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51725
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51725
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS51725
• View ligand binding statistics of PS51725
• Matching PDB structures: 1Q8B 1R6Y 1SQE 1TUV ... [ALL]

1	Authors	Sciara G., Kendrew S.G., Miele A.E., Marsh N.G., Federici L., Malatesta F., Schimperna G., Savino C., Vallone B.
	Title	The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.
	Source	EMBO J. 22:205-215(2003).
	PubMed ID	12514126
	DOI	10.1093/emboj/cdg031

2	Authors	Adams M.A., Jia Z.
	Title	Structural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli: identification of a novel quinol monooxygenase.
	Source	J. Biol. Chem. 280:8358-8363(2005).
	PubMed ID	15613473
	DOI	10.1074/jbc.M412637200

3	Authors	Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P., Schneewind O., Joachimiak A.
	Title	Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.
	Source	J. Biol. Chem. 280:2840-2846(2005).
	PubMed ID	15520015
	DOI	10.1074/jbc.M409526200

4	Authors	Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.P.
	Title	Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus.
	Source	J. Biol. Chem. 283:30957-30963(2008).
	PubMed ID	18713745
	DOI	10.1074/jbc.M709486200

5	Authors	Henrick K., Hirshberg M.
	Title	Structure of the signal transduction protein TRAP (target of RNAIII-activating protein).
	Source	Acta Crystallogr. F 68:744-750(2012).
	PubMed ID	22750855
	DOI	10.1107/S1744309112020167

6	Authors	Chim N., Iniguez A., Nguyen T.Q., Goulding C.W.
	Title	Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis.
	Source	J. Mol. Biol. 395:595-608(2010).
	PubMed ID	19917297
	DOI	10.1016/j.jmb.2009.11.025

7	Authors	Lemieux M.J., Ference C., Cherney M.M., Wang M., Garen C., James M.N.G. "The crystal structure of Rv0793, a hypothetical monooxygenase from M.
	Title	tuberculosis.
	Source	J. Struct. Funct. Genomics 6:245-257(2005).
	PubMed ID	16496224
	DOI	10.1007/s10969-005-9004-6

8	Authors	Wada T., Shirouzu M., Terada T., Kamewari Y., Park S.-Y., Tame J.R.H., Kuramitsu S., Yokoyama S.
	Title	Crystal structure of the conserved hypothetical protein TT1380 from Thermus thermophilus HB8.
	Source	Proteins 55:778-780(2004).
	PubMed ID	15103643
	DOI	10.1002/prot.20122

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