Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR000150 is a Cof family.
<p>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 [[cite:PUB00003337]]. 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.</p> <p>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) [[cite:PUB00053972]].</p> <p>E. coli YbiV ([swissprot:P75792]) also belongs to this group and has been experimentally characterised [[cite:PUB00028115]]. 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 α-β hydrolase domain that forms a Rossman fold, and an α-β domain. The active site is found in a negatively charged cavity found at the interface between the two domains.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
GO term | Namespace | Name | Definition | Relationships |
---|---|---|---|---|
Molecular function | Hydrolase activity | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3. |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | Haloacid dehalogenase-like hydrolase family protein isoform 2 [Theobroma cacao] gi|508782554|gb|EOY29810.1| | 24 | ||
– | Endoribonuclease YbeY; TAIR: AT2G25870.1 haloacid dehalogenase-like hydrolase family protein; Swiss-Prot: sp|Q5XD45|Y533_STRP6 Putative phosphatase M6_Spy0533; TrEMBL-Plants: tr|I1M9Z5|I1M9Z5_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0222600 | 26 | ||
– | Endoribonuclease YbeY; TAIR: AT2G25870.1 haloacid dehalogenase-like hydrolase family protein; Swiss-Prot: sp|Q5XD45|Y533_STRP6 Putative phosphatase M6_Spy0533; TrEMBL-Plants: tr|A0A0B2SRP5|A0A0B2SRP5_GLYSO Putative rRNA maturation factor; Found in the gene: LotjaGi1g1v0222600 | 26 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
cd07516 | CDD | 1 | 33.33 |