Summary: Methane/Phenol/Toluene Hydroxylase
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Methane/Phenol/Toluene Hydroxylase Provide feedback
Bacterial phenol hydroxylase is a multicomponent enzyme that catabolises phenol and some of its methylated derivatives. This Pfam family contains both the P1 and P3 polypeptides of phenol hydroxylase and the alpha and beta chain of methane hydroxylase protein A.
Herrmann H, Muller C, Schmidt I, Mahnke J, Petruschka L, Hahnke K; , Mol Gen Genet 1995;247:240-246.: Localization and organization of phenol degradation genes of Pseudomonas putida strain H. PUBMED:7753034 EPMC:7753034
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003430Bacterial phenol hydroxylase (EC) is a multicomponent enzyme that catabolises phenol and some of its methylated derivatives. This family contains both the P1 and P3 polypeptides of phenol hydroxlase and the alpha and beta chain of methane hydroxylase protein A. Methane hydroxylase protein A (EC) is responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyses the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. Also included in this family is toluene-4-monooxygenase system protein A (EC), which hydroxylates toluene to form P-cresol.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||cellular aromatic compound metabolic process (GO:0006725)|
|oxidation-reduction process (GO:0055114)|
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The members of this clan all share a distinctive four helical bundle. The four helices are arranged antiparallel with a left-handed twist. This helical bundle is distinguished from others by the long connection between the second and third helices. Some of the members contain a Fe or Mn dimer at the centre of the helical bundle. The ferritin fold was first described by Murzin AG and Chothia C, Cur Opin Struc Biol 1992, 2:895-903.
The clan contains the following 19 members:Coat_F COQ7 DUF2202 DUF2383 DUF305 DUF4142 DUF4439 DUF892 FA_desaturase_2 Ferritin Ferritin-like Ferritin_2 MiaE MiaE_2 Mn_catalase PaaA_PaaC Phenol_Hydrox Ribonuc_red_sm Rubrerythrin
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Curation and family details
|Seed source:||Pfam-B_15166 (release 5.2) & Pfam-B_3223 (Release 7.5)|
|Author:||Mian N, Bateman A|
|Number in seed:||23|
|Number in full:||1141|
|Average length of the domain:||186.10 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||63.63 %|
|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:||13|
|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 Phenol_Hydrox domain has been found. There are 190 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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