{PDOC00543} {PS00623; GMC_OXRED_1} {PS00624; GMC_OXRED_2} {BEGIN} ********************************** * GMC oxidoreductases signatures * ********************************** The following FAD flavoproteins oxidoreductases have been found [1,2] to be evolutionary related. These enzymes, which are called 'GMC oxidoreductases', are listed below. - Glucose oxidase (EC 1.1.3.4) (GOX) from Aspergillus niger. Reaction catalyzed: glucose + oxygen -> delta-gluconolactone + hydrogen peroxide. - Methanol oxidase (EC 1.1.3.13) (MOX) from fungi. Reaction catalyzed: methanol + oxygen -> acetaldehyde + hydrogen peroxide. - Choline dehydrogenase (EC 1.1.99.1) (CHD) from bacteria. Reaction catalyzed: choline + acceptor -> betaine acetaldehyde + reduced acceptor. - Glucose dehydrogenase (GLD) (EC 1.1.99.10) from Drosophila. Reaction catalyzed: glucose + acceptor -> delta-gluconolactone + reduced acceptor. - L-sorbose 1-dehydrogenase (EC 1.1.99.32) (SDH) from Gluconobacter oxydans. Reaction catylzed: L-sorbose + acceptor = 1-dehydro-L-sorbose + reduced acceptor. - Cholesterol oxidase (CHOD) (EC 1.1.3.6) from Brevibacterium sterolicum and Streptomyces strain SA-COO. Reaction catalyzed: cholesterol + oxygen -> cholest-4-en-3-one + hydrogen peroxide. - AlkJ [3], an alcohol dehydrogenase from Pseudomonas oleovorans, which converts aliphatic medium-chain-length alcohols into aldehydes. - Cellobiose dehydrogenase (CDH) (EC 1.1.98.18) from Phanerochaete chrysosporium. This family also includes a lyase: - (R)-mandelonitrile lyase (EC 4.1.2.10) (hydroxynitrile lyase) from plants [4], an enzyme involved in cyanogenis, the release of hydrogen cyanide from injured tissues. These enzymes are proteins of size ranging from 556 (CHD) to 664 (MOX) amino acid residues which share a number of regions of sequence similarities. One of these regions, located in the N-terminal section, corresponds to the FAD ADP- binding domain. The function of the other conserved domains is not yet known; we have selected two of these domains as signature patterns. The first one is located in the N-terminal section of these enzymes, about 50 residues after the ADP-binding domain, while the second one is located in the central section. -Consensus pattern: [GA]-[RKNC]-x-[LIVW]-G(2)-[GST](2)-x-[LIVM]-[NH]-x(3)- [FYWA]-x(2)-[PAG]-x(5)-[DNESHQA] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [GS]-[PSTA]-x(2)-[ST]-[PS]-x-[LIVM](2)-x(2)-S-G-[LIVM]-G -Sequences known to belong to this class detected by the pattern: ALL, except for cholesterol oxidases. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: May 2008 / Text revised. [ 1] Cavener D.R. "GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities." J. Mol. Biol. 223:811-814(1992). PubMed=1542121 [ 2] Henikoff S., Henikoff J.G. "Protein family classification based on searching a database of blocks." Genomics 19:97-107(1994). PubMed=8188249 [ 3] van Beilen J.B., Eggink G., Enequist H., Bos R., Witholt B. Mol. Microbiol. 6:3121-3136(1992). [ 4] Cheng I.P., Poulton J.E. Plant Cell Physiol. 34:1139-1143(1993). -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}