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InterPro: IPR012078 Methane/phenol monooxygenase, hydroxylase component

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UniProtKB

Matches:

126 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR012078 MP_mOase_hydro

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000040	MMOH_comp	126
Signatures in BioMart

InterPro Relationships Help

Parent

IPR003430 Methane/phenol/toluene hydroxylase

Contains

IPR012348 Ribonucleotide reductase-related

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen

InterPro annotation

Entry Details in BioMart

Abstract

This group represents the hydroxylase component of methane monooxygenase (EC:1.14.13.25) and phenol 2-monooxygenase (EC:1.14.13.7). Please see the following relevant references: [1, 2, 3, 4].

Structural links Help

PDB - click here

SCOP: a.25.1.2

CATH: 1.10.620.20

Database links Help

Enzyme: EC:1.14.13

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012078

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 Open in usermanual
1.	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. 247 240-6 1995 [PubMed: 7753034] http://dx.doi.org/10.1007/BF00705655
2.	Tonge GM, Harrison DE, Higgins IJ. Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b. Biochem. J. 161 333-44 1977 [PubMed: 15544] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=15544
3.	Neujahr HY, Gaal A. Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum. Eur. J. Biochem. 58 351-7 1975 [PubMed: 810352] http://dx.doi.org/10.1111/j.1432-1033.1975.tb02381.x
4.	Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ. NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath). Biochemistry 43 11983-91 2004 [PubMed: 15379538] http://dx.doi.org/10.1021/bi049066n

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
	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