CATH Domain 1oqmB00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.550	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
	3.90.550.10	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Domain Context

CATH Clusters

Superfamily	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Functional Family	beta-1,4-galactosyltransferase 1

Enzyme Information

2.4.1.90	N-acetyllactosamine synthase. based on mapping to UniProt P08037 UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine. -!- The reaction is catalyzed by a component of EC 2.4.1.22, which is identical with EC 2.4.1.38, and by an enzyme from the Golgi apparatus of animal tissues. -!- Formerly EC 2.4.1.98.
2.4.1.38	Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase. based on mapping to UniProt P08037 UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide. -!- Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. -!- High activity is shown toward such residues in branched-chain polysaccharides when these are linked by beta-1,6 links to galactose residues; lower activity toward residues linked to galactose by beta- 1,3 links. -!- A component of EC 2.4.1.22.
2.4.1.22	Lactose synthase. based on mapping to UniProt P08037 UDP-alpha-D-galactose + D-glucose = UDP + lactose. -!- The enzyme is a complex of 2 proteins A and B. -!- In the absence of the B protein (alpha-lactalbumin) the enzyme catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine (cf. EC 2.4.1.90).
2.4.1.-	Hexosyltransferases. based on mapping to UniProt P08037

UniProtKB Entries (2)

P29752	LALBA_MOUSE Mus musculus Alpha-lactalbumin
P08037	B4GT1_BOVIN Bos taurus Beta-1,4-galactosyltransferase 1

PDB Structure

PDB	1OQM
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Structure-based design of beta 1,4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity. Ramakrishnan, B., Qasba, P.K. J.Biol.Chem.