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InterPro: IPR007867 Glucose-methanol-choline oxidoreductase, C-terminal

Protein matchesHelp
UniProtKB
Matches:
2913 proteins
AccessionHelp IPR007867 GMC_OxRtase_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011533 Choline dehydrogenase
IPR012132 Glucose-methanol-choline oxidoreductase
IPR012400 Long-chain fatty alcohol dehydrogenase
GO Term annotationHelp
Function GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases [1, 2]. These enzymes include a variety of proteins; choline dehydrogenase (CHD), methanol oxidase (MOX) and cellobiose dehydrogenase (EC:1.1.99.18) [3] which share a number of regions of sequence similarities. The function of this C-terminal conserved domain is not yet known.

Structural linksHelp
SCOP: c.3.1.2 , d.16.1.1
Database linksHelp
Enzyme: EC:1.1.99.1
PANDIT: PF05199
Blocks: IPB007867

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR007867 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P12676 Cholesterol oxidase

P18173 Glucose dehydrogenase [acceptor]

Q8BJ64 Choline dehydrogenase, mitochondrial

Q8NE62 Choline dehydrogenase, mitochondrial

Q9S746 Protein HOTHEAD

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR006311 Twin-arginine translocation pathway, signal sequence
IPR000172 Glucose-methanol-choline oxidoreductase, N-terminal
IPR007867 Glucose-methanol-choline oxidoreductase, C-terminal
IPR011533 Choline dehydrogenase
IPR017909 Twin arginine translocation signal, Tat
IPR012132 Glucose-methanol-choline oxidoreductase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Cavener DR.
GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.
J. Mol. Biol. 223 811-4 1992 [PubMed: 1542121]
http://dx.doi.org/10.1016/0022-2836(92)90992-S
2. Li J, Vrielink A, Brick P, Blow DM.
Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases.
Biochemistry 32 11507-15 1993 [PubMed: 8218217]
http://dx.doi.org/10.1021/bi00094a006
3. Henriksson G, Johansson G, Pettersson G.
A critical review of cellobiose dehydrogenases.
J. Biotechnol. 78 93-113 2000 [PubMed: 10725534]
http://dx.doi.org/10.1016/S0168-1656(00)00206-6

Additional ReadingHelp
Lario PI, Sampson N, Vrielink A.
Sub-atomic resolution crystal structure of cholesterol oxidase: what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity.
J. Mol. Biol. 326 2003 1635-50 [PubMed: 12595270]
http://dx.doi.org/10.1016/S0022-2836(03)00054-8
Lyubimov AY, Heard K, Tang H, Sampson NS, Vrielink A.
Distortion of flavin geometry is linked to ligand binding in cholesterol oxidase.
Protein Sci. 16 2007 2647-56 [PubMed: 18029419]
http://dx.doi.org/10.1110/ps.073168207
Lario PI, Vrielink A.
Atomic resolution density maps reveal secondary structure dependent differences in electronic distribution.
J. Am. Chem. Soc. 125 2003 12787-94 [PubMed: 14558826]
http://dx.doi.org/10.1021/ja0289954
Lyubimov AY, Lario PI, Moustafa I, Vrielink A.
Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment.
Nat. Chem. Biol. 2 2006 259-64 [PubMed: 16604066]
http://dx.doi.org/10.1038/nchembio784
Chen L, Lyubimov AY, Brammer L, Vrielink A, Sampson NS.
The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase.
Biochemistry 47 2008 5368-77 [PubMed: 18410129]
http://dx.doi.org/10.1021/bi800228w
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InterPro 23.1