The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_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 13: mannose-1-phosphate guanyltransferase beta

There are 4 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
Mannose-1-phosphate guanylyltransferase. [EC: 2.7.7.13]
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
  • The bacterial enzyme can also use ITP and dGTP as donors.
141 A0A024R2X1 A0A024R2X1 A0A178VW16 A0A178VW16 A0A1S9DLW5 A0A1S9DLW5 A0A1S9DLW5 A0A1S9DLW5 A0A1S9DLW5 A0A229XJ90
(131 more...)
UTP--glucose-1-phosphate uridylyltransferase. [EC: 2.7.7.9]
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.
    1 P74285
    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.
    1 Q58501
    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.
    1 Q58501
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