Summary
Ring hydroxylating beta subunit
This subunit has a similar structure to NTF-2 and scytalone dehydratase.
Literature references
-
Kauppi B, Lee K, Carredano E, Parales RE, Gibson DT, Eklund H, Ramaswamy S; , Structure 1998;6:571-586.: Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1, 2-dioxygenase. PUBMED:9634695
InterPro entry IPR000391
The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonhaem iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centres to a terminal dioxygenase PUBMED:1444257. Aromatic-ring-hydroxylating dioxygenases oxidise aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilise a mononuclear non-haem iron centre to catalyse the addition of dioxygen to their respective substrates.Naphthalene 1,2-dioxygenase (NDO) from Pseudomonas sp. NCIB9816-4 has a domain structure and iron coordination of the Rieske domain is very similar to that of the cytochrome bc1 domain. The active-site iron centre of one of the alpha subunits is directly connected by hydrogen bonds through a single amino acid, Asp205, to the Rieske [2Fe-2S] centre in a neighbouring alpha subunit. This may be the main route for electron transfer PUBMED:9634695.
Clan
This family is a member of clan NTF2 (CL0051), which contains the following 14 members:
CaMKII_AD DUF1348 DUF2358 DUF3225 LEH MBA1 MecA_N Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL Tim44Gene Ontology
| Molecular function | catalytic activity (GO:0003824) |
| Biological process | cellular aromatic compound metabolic process (GO:0006725) |
| oxidation reduction (GO:0055114) |
External database links
| PANDIT: | PF00866 |
| SCOP: | 1ndo |
| SYSTERS: | Ring_hydroxyl_B |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
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 HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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_771 (release 3.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 44 |
| Number in full: | 717 |
| Average length of the domain: | 139.10 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 81.44 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 145 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 Ring_hydroxyl_B domain has been found.
Loading structure mapping...
