Summary: UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain
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UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain Provide feedback
The UDP-glucose/GDP-mannose dehydrogenaseses 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 .
Roychoudhury S, May TB, Gill JF, Singh SK, Feingold DS, Chakrabarty AM; , J Biol Chem 1989;264:9380-9385.: Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa. PUBMED:2470755 EPMC:2470755
Campbell RE, Sala RF, van de Rijn I, Tanner ME; , J Biol Chem 1997;272:3416-3422.: Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol. PUBMED:9013585 EPMC:9013585
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This tab holds annotation information from the InterPro database.
InterPro entry 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, 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, 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].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)|
|NAD binding (GO:0051287)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Seed source:||Pfam-B_1105 (release 3.0)|
|Author:||Finn RD, Bateman A, Griffiths-Jones SR|
|Number in seed:||161|
|Number in full:||6858|
|Average length of the domain:||98.00 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||23.17 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the UDPG_MGDP_dh_C domain has been found. There are 103 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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