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InterPro: IPR003454 Monooxygenase component MmoB/DmpM

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128 proteins

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Accession

IPR003454 mOase_MmoB_DmpM

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.90.56.10	mOase_MmoB_DmpM	119
ProDom	PD004249	mOase_MmoB_DmpM	101
Pfam	PF02406	MmoB_DmpM	128
SuperFamily	SSF56029	MmoB_DmpM	127
Signatures in BioMart

GO Term annotation Help

Process

GO:0006725 cellular aromatic compound metabolic process

Function

GO:0004497 monooxygenase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family consists of monooxygenase components such as MmoB methane monooxygenase (EC:1.14.13.25) regulatory protein B. When MmoB is present at low concentration it converts methane monooxygenase from an oxidase to a hydroxylase and stabilises intermediates required for the activation of dioxygen [1]. Also found in this family is DmpM or Phenol hydroxylase (EC:1.14.13.7) protein component P2, this protein lacks redox co-factors and is required for optimal turnover of Phenol hydroxylase [2]. Phenol hydroxylase catabolises phenol and some of its methylated derivatives in the first step of phenol biodegradation, and is required for growth on phenol. The multicomponent enzyme is made up of P0, P1, P2, P3, P4 and P5 polypeptides.

Structural links Help

PDB - click here

SCOP: d.137.1.1

CATH: 3.90.56.10

Database links Help

PANDIT: PF02406

Blocks: IPB003454

Taxonomic coverage Help

Example proteins Help

P18797 Methane monooxygenase regulatory protein B

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003454	Monooxygenase component MmoB/DmpM
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Walters KJ, Gassner GT, Lippard SJ, Wagner G. Structure of the soluble methane monooxygenase regulatory protein B. Proc. Natl. Acad. Sci. U.S.A. 96 7877-82 1999 [PubMed: 10393915] http://dx.doi.org/10.1073/pnas.96.14.7877
2.	Qian H, Edlund U, Powlowski J, Shingler V, Sethson I. Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. Biochemistry 36 495-504 1997 [PubMed: 9012665] http://dx.doi.org/10.1021/bi9619233

Additional Reading Open in usermanual
	Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. Biochemistry 38 1999 5799-812 [PubMed: 10231531] http://dx.doi.org/10.1021/bi982992f
	Mitchell KH, Studts JM, Fox BG. Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity. Biochemistry 41 2002 3176-88 [PubMed: 11863457] http://dx.doi.org/10.1021/bi012036p
	Hemmi H, Studts JM, Chae YK, Song J, Markley JL, Fox BG. Solution structure of the toluene 4-monooxygenase effector protein (T4moD). Biochemistry 40 2001 3512-24 [PubMed: 11297417] http://dx.doi.org/10.1021/bi0013703
	Orville AM, Studts JM, Lountos GT, Mitchell KH, Fox BG. Crystallization and preliminary analysis of native and N-terminal truncated isoforms of toluene-4-monooxygenase catalytic effector protein. Acta Crystallogr. D Biol. Crystallogr. 59 2003 572-5 [PubMed: 12595730] http://dx.doi.org/10.1107/S0907444903000416
	Lountos GT, Mitchell KH, Studts JM, Fox BG, Orville AM. Crystal structures and functional studies of T4moD, the toluene 4-monooxygenase catalytic effector protein. Biochemistry 44 2005 7131-42 [PubMed: 15882052] http://dx.doi.org/10.1021/bi047459g

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