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InterPro: IPR007235 Glycosyl transferase, family 28, C-terminal

Protein matchesHelp
UniProtKB
Matches:
2517 proteins
AccessionHelp IPR007235 Glyco_trans_28_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR006009 N-acetylglucosaminyltransferase, MurG
IPR016683 Glycosyl transferase, family 28, RedA, predicted
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
GO:0030259 lipid glycosylation
Function GO:0016758 transferase activity, transferring hexosyl groups
GO:0030246 carbohydrate binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates (EC:2.4.1.-) and related proteins into distinct sequence based families has been described [1]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [2]. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.

Glycosyltransferase family 28 GT28 comprises enzymes with a number of known activities; 1,2-diacylglycerol 3-beta-galactosyltransferase (EC:2.4.1.46); 1,2-diacylglycerol 3-beta-glucosyltransferase (EC:2.4.1.157); beta-N-acetylglucosamine transferase (EC:2.4.1). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.

Structural linksHelp
SCOP: c.87.1.2
CATH: 3.40.50.2000
Database linksHelp
Enzyme: EC:2.4.1.227
CAZy: GT28
PANDIT: PF04101
Blocks: IPB007235
Pfam Clan: CL0113.9

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR007235 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A2YTP9 Probable monogalactosyldiacylglycerol synthase 2, chloroplastic

O81770 Monogalactosyldiacylglycerol synthase 1, chloroplastic

P53178 UDP-N-acetylglucosamine transferase subunit ALG13

Q9D8C3 UDP-N-acetylglucosamine transferase subunit ALG13 homolog

Q9NP73 UDP-N-acetylglucosamine transferase subunit ALG13 homolog

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR007235 Glycosyl transferase, family 28, C-terminal
IPR009695 Monogalactosyldiacylglycerol synthase
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Campbell JA, Davies GJ, Bulone V, Henrissat B.
A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.
Biochem. J. 326 ( Pt 3) 929-39 1997 [PubMed: 9334165]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9334165
2. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999

Additional ReadingHelp
Ha S, Walker D, Shi Y, Walker S.
The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis.
Protein Sci. 9 2000 1045-52 [PubMed: 10892798]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=10892798&action=stream&blobtype=pdf
Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S.
Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases.
Proc. Natl. Acad. Sci. U.S.A. 100 2003 845-9 [PubMed: 12538870]
http://dx.doi.org/10.1073/pnas.0235749100
Mengin-Lecreulx D, Texier L, Rousseau M, van Heijenoort J.
The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis.
J. Bacteriol. 173 1991 4625-36 [PubMed: 1649817]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1649817&action=stream&blobtype=pdf
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InterPro 23.1