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CATH Superfamily 3.90.550.10

Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 65187: Bifunctional protein GlmU

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
UDP-N-acetylglucosamine diphosphorylase. [EC: 2.7.7.23]
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine.
  • Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea.
  • The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157.
  • The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate.
 752 A0A023D5H3 A0A024BVZ6 A0A024C840 A0A059HXB9 A0A059IV85 A0A060PRZ0 A0A060Q0K6 A0A060Q9J5 A0A063X5E8 A0A066PW31
(742 more...)
Glucosamine-1-phosphate N-acetyltransferase. [EC: 2.3.1.157]
Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate.
  • The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23.
 732 A0A023D5H3 A0A024BVZ6 A0A024C840 A0A059HXB9 A0A059IV85 A0A060PRZ0 A0A060Q0K6 A0A060Q9J5 A0A063X5E8 A0A066PW31
(722 more...)
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase. [EC: 2.3.1.129]
(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D- glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)- N-acetyl-alpha-D-glucosamine.
  • Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli.
 1 Q92HU1
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