ABM domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

ABM
ABM
	crystal structure of putative antibiotic biosynthesis monooxygenase from bacillus cereus
Identifiers
Symbol	ABM
Pfam	PF03992
Pfam clan	CL0032
InterPro	IPR007138
SCOP2	1n5t / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

In molecular biology, the ABM domain is a protein domain that is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species, which can carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The structure of ActVA-Orf6 monooxygenase from Streptomyces coelicolor, which is involved in actinorhodin biosynthesis, reveals a dimeric alpha+beta barrel topology.^[1] There is also a conserved histidine that is likely to be an active site residue. In the S. coelicolor protein SCO1909 this domain occurs as a repeat.

References

^ Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B (January 2003). "The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis". EMBO J. 22 (2): 205–15. doi:10.1093/emboj/cdg031. PMC 140106. PMID 12514126.

This article incorporates text from the public domain Pfam and InterPro: IPR007138

[pmid12514126-1] Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B (January 2003). "The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis". EMBO J. 22 (2): 205–15. doi:10.1093/emboj/cdg031. PMC 140106. PMID 12514126.

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