Summary: Ring hydroxylating alpha subunit (catalytic domain)
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Ring hydroxylating alpha subunit (catalytic domain) Provide feedback
This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015879Aromatic ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols [PUBMED:1885518]. The complex has both hydroxylase and electron transfer components. The hydroxylase component is itself composed of two subunits: an alpha-subunit of about 50 kDa, and a beta-subunit of about 20 kDa. The electron transfer component is either composed of two subunits: a ferredoxin and a ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit. Sequence analysis of hydroxylase subunits of ring hydroxylating systems (including toluene, benzene and napthalene 1,2-dioxygenases) suggests they are derived from a common ancestor [PUBMED:1885518]. The alpha-subunit binds both a Rieske-like 2Fe-2S cluster and an iron atom: conserved Cys and His residues in the N-terminal region may provide 2Fe-2S ligands, while conserved His and Tyr residues may coordinate the iron. The beta subunit may be responsible for the substrate specificity of the dioxygenase system [PUBMED:1885518]. This entry represents the conserved C-terminal domain found in the alpha subunit of aromatic-ring-hydroxylating dioxygenases.
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The Bet_V_I family is composed of sequences related to the major Birch (Betula verrucose) pollen antigen Betv1. This allergen is known to cause hayfever, dermatitis, asthma and occasionally anaphylactic shock. The other families in this clan share the same structure as Betv1 which is composed of antiparallel beta sheets and alpha helices. There is a cavity between the beta sheet and a long C terminal helix. The cavity appears to play roles in the binding of lipid molecules  which seems a common feature of the families in this clan.
The clan contains the following 14 members:AHSA1 Aromatic_hydrox Bet_v_1 COXG DUF1857 DUF2505 DUF3074 DUF3211 DUF3284 IP_trans Polyketide_cyc Polyketide_cyc2 Ring_hydroxyl_A START
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_407 (release 3.0)|
|Number in seed:||128|
|Number in full:||4563|
|Average length of the domain:||206.60 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||58.44 %|
|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:||14|
|Download:||download the raw HMM for this family|
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There are 3 interactions 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 Ring_hydroxyl_A domain has been found. There are 110 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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