Summary: Homotrimeric ring hydroxylase
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Homotrimeric ring hydroxylase Provide feedback
This domain is found on aromatic hydroxylating enzymes such as 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida and carbazole 1,9a-dioxygenase from Janthinobacterium. These enzymes are homotrimers and are distantly related to the typical oxygenase . This domain is found C terminal to the Rieske domain which binds an iron-sulphur cluster.
Nojiri H, Ashikawa Y, Noguchi H, Nam JW, Urata M, Fujimoto Z, Uchimura H, Terada T, Nakamura S, Shimizu K, Yoshida T, Habe H, Omori T; , J Mol Biol. 2005;351:355-370.: Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase. PUBMED:16005887 EPMC:16005887
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This tab holds annotation information from the InterPro database.
InterPro entry IPR021028
This entry represents the catalytic domain from a family of homotrimeric enzymes that hydroxylate aromatic compounds, including 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida and carbazole 1,9a-dioxygenase from Janthinobacterium. The catalytic domain is found C-termnial to the iron-sulphur-binding Rieske domain and is composed of antiparallel beta sheets and alpha helices [PUBMED:16005887]. It is part of a much larger superfamily of lipid binding domains which form a common fold that works as a versatile scaffold for binding bulky ligands [PUBMED:18922149].
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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
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Curation and family details
|Seed source:||Pfam-B_24837 (release 22.0)|
|Author:||Radauer C, Mistry J|
|Number in seed:||7|
|Number in full:||55|
|Average length of the domain:||216.30 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||59.09 %|
|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:||3|
|Download:||download the raw HMM for this family|
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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 Aromatic_hydrox domain has been found. There are 49 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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