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InterPro: IPR015920 Cellobiose dehydrogenase, cytochrome

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171 proteins

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Accession

IPR015920 Cellobiose_DH_cyt

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.40.1210	Cellobiose_DH_cyt	171
Signatures in BioMart

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Parent

IPR008960 Carbohydrate-binding domain family 9-like

InterPro annotation

Entry Details in BioMart

Abstract

Cellobiose dehydrogenase (CHD; EC:1.1.99.18) is found in a variety of fungi, including white rot, brown rot and plant pathogen fungi. The enzyme is extracellular flavocytochrome that degrades both cellulose and lignin. It acts as a monomer consisting of two domains: a cytochrome domain containing a b-type haem, which is linked through a peptide linker to a large flavodehydrogenase domain containing FAD as a cofactor [1].

This entry represents the b-type cytochrome domain. This domain assumes an immunoglobulin-like beta-sandwich fold consisting of 7 beta-strands in 2 sheets with a Greek key topology; the haem iron is ligated by a Met/His couple and is docked at the exterior of the enzyme [2].

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SCOP: b.1.9.1

CATH: 2.60.40.1210

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Overlapping InterPro entries Help

IPR015920

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q01738 Cellobiose dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
IPR007867	Glucose-methanol-choline oxidoreductase, C-terminal
IPR015920	Cellobiose dehydrogenase, cytochrome
IPR008960	Carbohydrate-binding domain family 9-like
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Igarashi K, Verhagen MF, Samejima M, Schulein M, Eriksson KE, Nishino T. Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. A flavohemoprotein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor. J. Biol. Chem. 274 3338-44 1999 [PubMed: 9920875] http://dx.doi.org/10.1074/jbc.274.6.3338
2.	Hallberg BM, Bergfors T, Backbro K, Pettersson G, Henriksson G, Divne C. A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase. Structure 8 79-88 2000 [PubMed: 10673428] http://dx.doi.org/10.1016/S0969-2126(00)00082-4

Additional Reading Open in usermanual
	Rotsaert FA, Hallberg BM, de Vries S, Moenne-Loccoz P, Divne C, Renganathan V, Gold MH. Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase. J. Biol. Chem. 278 2003 33224-31 [PubMed: 12796496] http://dx.doi.org/10.1074/jbc.M302653200

InterPro 24.0