Methanol dehydrogenase subunit superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: All alpha proteins [ 46456] (284)
• Fold: Non-globular all-alpha subunits of globular proteins [ 48661] (14)
• Superfamily: Methanol dehydrogenase subunit [ 48666]
• Families: Methanol dehydrogenase subunit [ 48667]

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Superfamily statistics

	Genomes (28)	Uniprot 2018_03 genome	PDB chains (SCOP 1.75)
Domains	28	162	3
Proteins	28	162	3

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Functional annotation

• General category: Metabolism
• Detailed category: Coenzyme metabolism and transport

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Enzyme Commission (EC)

Highlighted in gray are those with FDR_all>0.001

	EC term	FDR (all)	IC level	SDEC level	Annotation (direct or inherited)
Enzyme Commission (EC)	With a cytochrome as acceptor	0	2.253	--	DIRECT
Enzyme Commission (EC)	Methanol dehydrogenase (cytochrome c)	0	2.952	--	DIRECT
Enzyme Commission (EC)	Oxidoreductases	0	0.6234	Least Informative	DIRECT
Enzyme Commission (EC)	Acting on the CH-OH group of donors	0	1.228	Moderately Informative	DIRECT

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InterPro annotation

• Cross references: IPR003420 SSF48666 Protein matches
• Abstract:

  Methanol dehydrogenase (MDH) , found in Gram-negative bacteria, is a pyrroloquinoline quinone (PQQ)-containing enzyme which oxidises methanol to formaldehyde. It is located in the periplasmic space and passes electrons derived from the oxidation of methanol to the soluble cytochrome cL [15234264]. The enzyme is a tetramer composed of two large alpha subunits and two smaller beta subunits. The alpha subunit binds the PQQ cofactor and contains the active site, while the function of the beta subunit is currently unknown [11502173]. The alpha subunit forms an eight-bladed propeller structure, with several novel tryptophan-docking motifs linking the individual blades together.

  This entry represents the beta subunit of methanol dehydrogenase.

InterPro database

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