SMART: Pfam domain ABM

The domain within your query sequence starts at position 251 and ends at position 326; the E-value for the ABM domain shown below is 2.1e-14.

IMLVQRQMSVTEEDLEEFQLALKHYVESASAQSGCLRISIQKLSNESRYMIYEFWENSSV
WNRHLQTNYSKTFQRS

ABM

PFAM accession number:	PF03992
Interpro abstract (IPR007138):	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 [ (PUBMED:12514126) ]. Escherichia coli probable quinol monooxygenase YgiN, can oxidize menadiol to menadione [ (PUBMED:15613473) ]. Staphylococcus aureus heme-degrading enzymes IsdG and IsdI [ (PUBMED:15520015) (PUBMED:18713745) ]. Staphylococci signal transduction protein TRAP (target of RNAIII- activating protein) [ (PUBMED:22750855) ]. Mycobacterium tuberculosis heme-degrading monooxygenase MhuD (or Rv3592) [ (PUBMED:19917297) ]. 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 [ (PUBMED:16496224) ]. Thermus thermophilus hypothetical protein TT1380 [ (PUBMED:15103643) ]. 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 [ (PUBMED:15103643) ]. 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 [ (PUBMED:12514126) (PUBMED:15613473) (PUBMED:15520015) (PUBMED:22750855) (PUBMED:16496224) (PUBMED:15103643) ].

PFAM accession number:

PF03992

Interpro abstract (IPR007138):

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 [ (PUBMED:12514126) ].
Escherichia coli probable quinol monooxygenase YgiN, can oxidize menadiol to menadione [ (PUBMED:15613473) ].
Staphylococcus aureus heme-degrading enzymes IsdG and IsdI [ (PUBMED:15520015) (PUBMED:18713745) ].
Staphylococci signal transduction protein TRAP (target of RNAIII- activating protein) [ (PUBMED:22750855) ].
Mycobacterium tuberculosis heme-degrading monooxygenase MhuD (or Rv3592) [ (PUBMED:19917297) ].
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 [ (PUBMED:16496224) ].
Thermus thermophilus hypothetical protein TT1380 [ (PUBMED:15103643) ].

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 [ (PUBMED:15103643) ]. 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 [ (PUBMED:12514126) (PUBMED:15613473) (PUBMED:15520015) (PUBMED:22750855) (PUBMED:16496224) (PUBMED:15103643) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ABM