UDPG_MGDP_dh_CUDP binding domain
|SMART accession number:||SM00984|
|Description:||The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate (PUBMED:2470755), (PUBMED:9013585).|
|Interpro abstract (IPR014027):|
The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate [(PUBMED:2470755), (PUBMED:9013585)].
The enzymes have a wide range of functions. In plants UDP-glucose dehydrogenase, EC 220.127.116.11, is an important enzyme in the synthesis of hemicellulose and pectin [(PUBMED:12031484)], which are the components of newly formed cell walls; while in zebrafish UDP-glucose dehydrogenase is required for cardiac valve formation [(PUBMED:11533493)]. In Xanthomonas campestris, a plant pathogen, UDP-glucose dehydrogenase is required for virulence [(PUBMED:11554764)].
GDP-mannose dehydrogenase, EC 18.104.22.168, catalyses the formation of GDP-mannuronic acid, which is the monomeric unit from which the exopolysaccharide alginate is formed. Alginate is secreted by a number of bacteria, which include Pseudomonas aeruginosa and Azotobacter vinelandii. In P. aeruginosa, alginate is believed to play an important role in the bacteria's resistance to antibiotics and the host immune response [(PUBMED:12135385)], while in A. vinelandii it is essential for the encystment process [(PUBMED:9864323)].
This entry represents the C-terminal substrate-binding domain of these enzymes. Structural studies indicate that this domain forms an incomplete dinucleotide binding fold [(PUBMED:10841783), (PUBMED:12705829)].
|GO process:||oxidation-reduction process (GO:0055114)|
|GO function:||NAD binding (GO:0051287), oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)|
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