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InterPro: IPR013476 Methylamine dehydrogenase heavy chain

Protein matches Help

UniProtKB

Matches:

9 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

IPR013476 MeN_DH_hvc

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF017797	TTQ_MADH_Hv	7
TIGRFAMs	TIGR02658	TTQ_MADH_Hv	9
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009451 Methylamine dehydrogenase heavy subunit

Contains

IPR011044 Quinoprotein amine dehydrogenase, beta chain-like
IPR015943 WD40/YVTN repeat-like-containing domain

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 is a periplasmic enzyme found in Gram-negative methylotrophs [1]. It is induced when grown on methylamine as a growth substrate and catalyses the oxidative deamination of primary amines to their corresponding aldehydes.

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

PRIAM: PRI001651

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013476

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

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
	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 1998 131-49 [PubMed: 9514722] http://dx.doi.org/10.1006/jmbi.1997.1511
	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 24.0