Summary: MmoB/DmpM family
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
MmoB/DmpM family Provide feedback
This family consists of monooxygenase components such as MmoB methane monooxygenase ( EC:1.14.13.25) regulatory protein B. When MmoB is present at low concentration it converts methane monooxygenase from an oxidase to a hydroxylase and stabilises intermediates required for the activation of dioxygen [1]. Also found in this family is DmpM or Phenol hydroxylase ( EC:1.14.13.7) protein component P2, this protein lacks redox co-factors and is required for optimal turnover of Phenol hydroxylase [3].
Literature references
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Walters KJ, Gassner GT, Lippard SJ, Wagner G; , Proc Natl Acad Sci U S A 1999;96:7877-7882.: Structure of the soluble methane monooxygenase regulatory protein B. PUBMED:10393915 EPMC:10393915
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Chang SL, Wallar BJ, Lipscomb JD, Mayo KH; , Biochemistry 1999;38:5799-5812.: Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. PUBMED:10231531 EPMC:10231531
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Qian H, Edlund U, Powlowski J, Shingler V, Sethson I; , Biochemistry 1997;36:495-504.: Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. PUBMED:9012665 EPMC:9012665
External database links
| PANDIT: | PF02406 |
| Pseudofam: | PF02406 |
| SCOP: | 1hqi |
| SYSTERS: | MmoB_DmpM |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003454
This family consists of monooxygenase components such as MmoB methane monooxygenase (EC) regulatory protein B. When MmoB is present at low concentration it converts methane monooxygenase from an oxidase to a hydroxylase and stabilises intermediates required for the activation of dioxygen [PUBMED:10393915]. Also found in this family is DmpM or Phenol hydroxylase (EC) protein component P2, this protein lacks redox co-factors and is required for optimal turnover of Phenol hydroxylase [PUBMED:9012665]. Phenol hydroxylase catabolises phenol and some of its methylated derivatives in the first step of phenol biodegradation, and is required for growth on phenol. The multicomponent enzyme is made up of P0, P1, P2, P3, P4 and P5 polypeptides.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | monooxygenase activity (GO:0004497) |
| Biological process | cellular aromatic compound metabolic process (GO:0006725) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (40) |
Full (224) |
Representative proteomes | NCBI (207) |
Meta (3) |
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| RP15 (29) |
RP35 (57) |
RP55 (73) |
RP75 (81) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (40) |
Full (224) |
Representative proteomes | NCBI (207) |
Meta (3) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (29) |
RP35 (57) |
RP55 (73) |
RP75 (81) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_1148 (release 5.2) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bashton M, Bateman A |
| Number in seed: | 40 |
| Number in full: | 224 |
| Average length of the domain: | 87.60 aa |
| Average identity of full alignment: | 31 % |
| Average coverage of the sequence by the domain: | 82.55 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 87 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
MmoB_DmpMStructures
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 MmoB_DmpM domain has been found. There are 27 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence