Summary: Antibiotic biosynthesis monooxygenase
This is the Wikipedia entry entitled "ABM domain". More...
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ABM domain Edit Wikipedia article
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crystal structure of putative antibiotic biosythesis monooxygenase from bacillus cereus
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. 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.
Antibiotic biosynthesis monooxygenase Provide feedback
This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 (Q9X9W3) is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.
Internal database links
|Similarity to PfamA using HHSearch:||Dabb DUF3291|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007138
This domain 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 (SWISSPROT), which is involved in actinorhodin biosynthesis, reveals a dimeric alpha+beta barrel topology [PUBMED:12514126]. There is also a conserved histidine that is likely to be an active site residue. In S. coelicolor SCO1909 (SWISSPROT) this domain occurs as a repeat.
This domain is also found in protein LsrG, involved in the degradation of quorum-sensing molecule autoinducer-2 [PUBMED:17274596], and in several uncharacterised proteins.
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This superfamily of proteins possess a Ferredoxin-like fold. Pairs of these assemble into a beta barrel. The function of this barrel is quite varied and includes Muconolactone isomerase as well as monooxygenases.
The clan contains the following 18 members:ABM AsnC_trans_reg Chlor_dismutase Dabb Dehydratase_hem DUF1330 DUF3291 DUF4188 DUF718 DUF881 Dyp_perox EthD MIase MmlI NapD NIPSNAP SOR YCII
We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Yeats C|
|Number in seed:||114|
|Number in full:||8140|
|Average length of the domain:||77.50 aa|
|Average identity of full alignment:||17 %|
|Average coverage of the sequence by the domain:||63.08 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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The tree shows the occurrence of this domain across different species. More...
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ABM domain has been found. There are 85 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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