Family

Cof family (IPR000150)

Short name: Cof

Family relationships

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 [PMID: 7966317]. 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 coli contains a total of six proteins from this entry. Sequence similarities suggest that these enzymes are phosphatases which work on phosphorylated sugars.

This entry represents a family belonging to the HAD superfamily. It is named after E. coli Cof and is notable for the large number of paralogues in many species. Cof is a phosphatase that catalyzes the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate) to HMP-P (4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate) [PMID: 15292217].

E. coli YbiV (P75792) also belongs to this group and has been experimentally characterised [PMID: 15657928]. 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.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016787 hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
TIGRFAMs