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InterPro: IPR017476 Nucleotide sugar dehydrogenase

Protein matchesHelp
UniProtKB
Matches:
2945 proteins
AccessionHelp IPR017476 Nucleotide_sugar_DH
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001732 UDP-glucose/GDP-mannose dehydrogenase, N-terminal
IPR014026 UDP-glucose/GDP-mannose dehydrogenase, dimerisation
IPR014027 UDP-glucose/GDP-mannose dehydrogenase, C-terminal
IPR014028 UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding domain
InterPro annotation
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AbstractHelp

Enzymes in this family catalyse the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (EC:1.1.1.22) [1], GDP-mannose 6-dehydrogenase (EC:1.1.1.132) [2], UDP-N-acetylglucosamine 6-dehydrogenase (EC:1.1.1.136) [3], UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase [4] and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase [5]. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three domains, IPR001732, IPR014026, and IPR014027 for the N-terminal, central, and C-terminal regions respectively.

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Database linksHelp
Enzyme: EC:1.1.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017476 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O02373 UDP-glucose 6-dehydrogenase

O60701 UDP-glucose 6-dehydrogenase

O70475 UDP-glucose 6-dehydrogenase

Q19905 UDP-glucose 6-dehydrogenase

Q9FM01 Probable UDP-glucose 6-dehydrogenase 2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR008927 6-phosphogluconate dehydrogenase, C-terminal-like
IPR016040 NAD(P)-binding domain
IPR014028 UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding domain
IPR014027 UDP-glucose/GDP-mannose dehydrogenase, C-terminal
IPR014026 UDP-glucose/GDP-mannose dehydrogenase, dimerisation
IPR001732 UDP-glucose/GDP-mannose dehydrogenase, N-terminal
IPR017476 Nucleotide sugar dehydrogenase
SWISS-MODEL
PDB Chain
ModBase
CATH Domain

PublicationsHelp
1. Pagni M, Lazarevic V, Soldo B, Karamata D.
Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in teichuronic acid synthesis.
Microbiology (Reading, Engl.) 145 ( Pt 5) 1049-53 1999 [PubMed: 10376820]
2. Campos M, Martinez-Salazar JM, Lloret L, Moreno S, Nunez C, Espin G, Soberon-Chavez G.
Characterization of the gene coding for GDP-mannose dehydrogenase (algD) from Azotobacter vinelandii.
J. Bacteriol. 178 1793-9 1996 [PubMed: 8606150]
http://jb.asm.org/cgi/content/abstract/178/7/1793
3. Miller WL, Wenzel CQ, Daniels C, Larocque S, Brisson JR, Lam JS.
Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1.
J. Biol. Chem. 279 37551-8 2004 [PubMed: 15226302]
http://dx.doi.org/10.1074/jbc.M404749200
4. Zhao X, Creuzenet C, Belanger M, Egbosimba E, Li J, Lam JS.
WbpO, a UDP-N-acetyl-D-galactosamine dehydrogenase from Pseudomonas aeruginosa serotype O6.
J. Biol. Chem. 275 33252-9 2000 [PubMed: 10931835]
http://dx.doi.org/10.1074/jbc.M004191200
5. Meier-Dieter U, Starman R, Barr K, Mayer H, Rick PD.
Biosynthesis of enterobacterial common antigen in Escherichia coli. Biochemical characterization of Tn10 insertion mutants defective in enterobacterial common antigen synthesis.
J. Biol. Chem. 265 13490-7 1990 [PubMed: 2166030]
http://intl.jbc.org/cgi/content/abstract/265/23/13490

Additional ReadingHelp
Snook CF, Tipton PA, Beamer LJ.
Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa.
Biochemistry 42 2003 4658-68 [PubMed: 12705829]
http://dx.doi.org/10.1021/bi027328k
Campbell RE, Mosimann SC, van De Rijn I, Tanner ME, Strynadka NC.
The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation.
Biochemistry 39 2000 7012-23 [PubMed: 10841783]
http://dx.doi.org/10.1021/bi000181h
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InterPro 23.1