| Type: | Family | Name: | Cof protein |
| Description: | The Haloacid Dehydrogenase (HAD) superfamily includes phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, which are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification []. Proteins in this entry are mostly uncharacterised, though they form a distinct subgroup within the HAD superfamily. Members are found almost exclusively in bacteria and many species contain several paralogs, for example Escherichia colicontains a total of six proteins from this entry. Sequence similarities suggest that these enzymes are phosphatases which work on phosphorylated sugars.The YbiV () protein from E. coli has been experimentally characterised []. This enzyme catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. It has a wide substrate specificity, catalyzing the hydrolysis of ribose-5-phosphate and glucose-6-phosphate most efficiently, but it is not known if these are the real substrates in vivo. The protein appears to be a monomer that contains two domains, an alpha-beta hydrolase domain that forms a Rossman fold, and an alpha-beta domain. The active site is found in a negatively charged cavity found at the interface between the two domains. | Short Name: | Hypothet_cof |
