3-deoxy-D-manno-octulosonic-acid transferase; Reviewed

3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis].

3-Deoxy-D-manno-octulosonic-acid transferase (kdotransferase). Members of this family transfer activated sugars to a variety of substrates, including glycogen, fructose-6-phosphate and lipopolysaccharides. Members of the family transfer UDP, ADP, GDP or CMP linked sugars. The Glycos_transf_N region is flanked at the N-terminus by a signal peptide and at the C-terminus by Glycos_transf_1 (pfam00534). The eukaryotic glycogen synthases may be distant members of this bacterial family.

phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.

Membrane-embeddedmonofunctional glycosyltransferase WaaA of Aquifex aeolicus, substrate-free form [Aquifex aeolicus],2XCI_B Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, substrate-free form [Aquifex aeolicus],2XCI_C Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, substrate-free form [Aquifex aeolicus],2XCI_D Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, substrate-free form [Aquifex aeolicus],2XCU_A Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP [Aquifex aeolicus],2XCU_B Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP [Aquifex aeolicus],2XCU_C Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP [Aquifex aeolicus],2XCU_D Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP [Aquifex aeolicus]

ChainA, 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE [Acinetobacter baumannii]

3-deoxy-D-manno-octulosonic acid transferase OS=Escherichia coli (strain K12) OX=83333 GN=waaA PE=1 SV=1

3-deoxy-D-manno-octulosonic acid transferase OS=Escherichia coli O157:H7 OX=83334 GN=waaA PE=3 SV=1

3-deoxy-D-manno-octulosonic acid transferase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=waaA PE=3 SV=1

3-deoxy-D-manno-octulosonic acid transferase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=waaA PE=1 SV=1

Bifunctional glycosyltransferase/methyltransferase OS=Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) OX=190304 GN=trmB PE=3 SV=1