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InterPro: IPR009451 Methylamine dehydrogenase heavy subunit

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UniProtKB

Matches:

50 proteins

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

Accession

IPR009451 Metamine_DH_Hsu

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF06433	Me-amine-dh_H	50
Signatures in BioMart

InterPro Relationships Help

Children

IPR013476 Methylamine dehydrogenase heavy chain

Contains

IPR011044 Quinoprotein amine dehydrogenase, beta chain-like

GO Term annotation Help

Process

GO:0030416 methylamine metabolic process
GO:0055114 oxidation reduction

Function

GO:0030058 amine dehydrogenase activity

Component

GO:0042597 periplasmic space

InterPro annotation

Entry Details in BioMart

Abstract

Methylamine dehydrogenase (EC:1.4.99.3) is a periplasmic quinoprotein found in several methyltrophic bacteria [1]. It is induced when grown on methylamine as a carbon source MADH and catalyses the oxidative deamination of amines to their corresponding aldehydes. The redox cofactor of this enzyme is tryptophan tryptophylquinone (TTQ). Electrons derived from the oxidation of methylamine are passed to an electron acceptor, which is usually the blue-copper protein amicyanin (IPR002386).

RCH2NH2 + H2O + acceptor = RCHO + NH3 + reduced acceptor

MADH is a hetero-tetramer, comprised of two heavy subunits and two light subunits. The heavy subunit forms a seven-bladed beta-propeller like structure [2].

Structural links Help

PDB - click here

SCOP: b.69.2.1

CATH: 2.130.10.10

Database links Help

Enzyme: EC:1.4.99.3

PANDIT: PF06433

Pfam Clan: CL0186.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR009451

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P23006 Methylamine dehydrogenase heavy chain

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011044	Quinoprotein amine dehydrogenase, beta chain-like
IPR013476	Methylamine dehydrogenase heavy chain
IPR009451	Methylamine dehydrogenase heavy subunit
IPR015943	WD40/YVTN repeat-like-containing domain
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Chistoserdov AY, Chistoserdova LV, McIntire WS, Lidstrom ME. Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants. J. Bacteriol. 176 4052-65 1994 [PubMed: 8021187] http://jb.asm.org/cgi/content/abstract/176/13/4052
2.	Chen L, Doi M, Durley RC, Chistoserdov AY, Lidstrom ME, Davidson VL, Mathews FS. Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution. J. Mol. Biol. 276 131-49 1998 [PubMed: 9514722] http://dx.doi.org/10.1006/jmbi.1997.1511

Additional Reading Open in usermanual
	Sun D, Chen ZW, Mathews FS, Davidson VL. Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin. Biochemistry 41 2002 13926-33 [PubMed: 12437349] http://dx.doi.org/10.1021/bi026654x
	Chen L, Durley RC, Mathews FS, Davidson VL. Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Science 264 1994 86-90 [PubMed: 8140419] http://www.sciencemag.org/cgi/content/abstract/264/5155/86
	Huizinga EG, van Zanten BA, Duine JA, Jongejan JA, Huitema F, Wilson KS, Hol WG. Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry 31 1992 9789-95 [PubMed: 1390754] http://dx.doi.org/10.1021/bi00155a036

InterPro 23.1