{PDOC51725}
{PS51725; ABM}
{BEGIN}
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* ABM domain profile *
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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 alpha-helices (H1-3) and four beta-strands (S1-4)
and has  a ferredoxin-like split BetaAlphaBeta-fold with an antiparallel beta-
sheet (see  <1IUJ>).  The  beta-sheets of two monomers form a 10-strand, anti-
parallel beta-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 2014 / First entry.

[ 1] 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."
     EMBO J. 22:205-215(2003).
     PubMed=12514126; DOI=10.1093/emboj/cdg031
[ 2] Adams M.A., Jia Z.
     "Structural and biochemical evidence for an enzymatic quinone redox
     cycle in Escherichia coli: identification of a novel quinol
     monooxygenase."
     J. Biol. Chem. 280:8358-8363(2005).
     PubMed=15613473; DOI=10.1074/jbc.M412637200
[ 3] Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P.,
     Schneewind O., Joachimiak A.
     "Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with
     structural similarity to monooxygenases."
     J. Biol. Chem. 280:2840-2846(2005).
     PubMed=15520015; DOI=10.1074/jbc.M409526200
[ 4] Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.P.
     "Ruffling of metalloporphyrins bound to IsdG and IsdI, two
     heme-degrading enzymes  in Staphylococcus aureus."
     J. Biol. Chem. 283:30957-30963(2008).
     PubMed=18713745; DOI=10.1074/jbc.M709486200
[ 5] Henrick K., Hirshberg M.
     "Structure of the signal transduction protein TRAP (target of
     RNAIII-activating protein)."
     Acta Crystallogr. F 68:744-750(2012).
     PubMed=22750855; DOI=10.1107/S1744309112020167
[ 6] Chim N., Iniguez A., Nguyen T.Q., Goulding C.W.
     "Unusual diheme conformation of the heme-degrading protein from
     Mycobacterium tuberculosis."
     J. Mol. Biol. 395:595-608(2010).
     PubMed=19917297; DOI=10.1016/j.jmb.2009.11.025
[ 7] 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.
     tuberculosis."
     J. Struct. Funct. Genomics 6:245-257(2005).
     PubMed=16496224; DOI=10.1007/s10969-005-9004-6
[ 8] Wada T., Shirouzu M., Terada T., Kamewari Y., Park S.-Y., Tame J.R.H.,
     Kuramitsu S., Yokoyama S.
     "Crystal structure of the conserved hypothetical protein TT1380 from
     Thermus thermophilus HB8."
     Proteins 55:778-780(2004).
     PubMed=15103643; DOI=10.1002/prot.20122

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