PROSITE documentation PDOC51725ABM 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.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 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. |
| Title | The crystal structure of Rv0793, a hypothetical monooxygenase from M. 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 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)