EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR003430 Methane/phenol/toluene hydroxylase

Protein matches Help

UniProtKB

Matches:

799 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003430 Phenol_Hydrox

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02332	Phenol_Hydrox	799
Signatures in BioMart

InterPro Relationships Help

Children

IPR012078 Methane/phenol monooxygenase, hydroxylase component

Contains

IPR012348 Ribonucleotide reductase-related

GO Term annotation Help

Process

GO:0006725 cellular aromatic compound metabolic process
GO:0055114 oxidation reduction

InterPro annotation

Entry Details in BioMart

Abstract

Bacterial phenol hydroxylase (EC:1.14.13.7) 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:1.14.13.25) 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:1.14.13), which hydroxylates toluene to form P-cresol.

Structural links Help

PDB - click here

SCOP: a.25.1.2

CATH: 1.10.620.20

Database links Help

Enzyme: EC:1.14.13

PANDIT: PF02332

Blocks: IPB003430

COMe: PRX001038

Pfam Clan: CL0044.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003430

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P18798 Methane monooxygenase component A beta chain

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR009078	Ferritin/ribonucleotide reductase-like
IPR003430	Methane/phenol/toluene hydroxylase
IPR012348	Ribonucleotide reductase-related
IPR012078	Methane/phenol monooxygenase, hydroxylase component
	PDB Chain
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Sazinsky MH, Lippard SJ. Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the alpha-subunit. J. Am. Chem. Soc. 127 2005 5814-25 [PubMed: 15839679] http://dx.doi.org/10.1021/ja044099b
	Murray LJ, Garcia-Serres R, McCormick MS, Davydov R, Naik SG, Kim SH, Hoffman BM, Huynh BH, Lippard SJ. Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase. Biochemistry 46 2007 14795-809 [PubMed: 18044971] http://dx.doi.org/10.1021/bi7017128
	Sazinsky MH, Bard J, Di Donato A, Lippard SJ. Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases. J. Biol. Chem. 279 2004 30600-10 [PubMed: 15096510] http://dx.doi.org/10.1074/jbc.M400710200
	Herrmann H, Muller C, Schmidt I, Mahnke J, Petruschka L, Hahnke K. Localization and organization of phenol degradation genes of Pseudomonas putida strain H. Mol. Gen. Genet. 247 1995 240-6 [PubMed: 7753034] http://dx.doi.org/10.1007/BF00705655
	McCormick MS, Sazinsky MH, Condon KL, Lippard SJ. X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior. J. Am. Chem. Soc. 128 2006 15108-10 [PubMed: 17117860] http://dx.doi.org/10.1021/ja064837r
	Sazinsky MH, Merkx M, Cadieux E, Tang S, Lippard SJ. Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath). Biochemistry 43 2004 16263-76 [PubMed: 15610020] http://dx.doi.org/10.1021/bi048140z

InterPro 23.1