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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 64919: Lipopolysaccharide core biosynthesis glycosyltrans...

There are 2 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
Shikimate dehydrogenase. [EC: 1.1.1.25]
Shikimate + NADP(+) = 3-dehydroshikimate + NADPH.
  • NAD(+) cannot replace NADP(+).
  • In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10.
 7 A0A085U3Q5 A0A0E1NL11 A0A0H3NJR6 A0A0H3PK37 A4N0M3 A4P0V8 F4MWW4
Glucosyl-3-phosphoglycerate synthase. [EC: 2.4.1.266]
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)- 3-phospho-D-glycerate.
  • The enzyme is involved in biosynthesis of 2-O-(alpha-D- glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyzes the conversion of GDP- glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)- 3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D- glucopyranosyl)-D-glycerate by EC 3.1.3.85.
  • The activity is dependent on divalent cations (Mn(2+), Co(2+), or Mg(2+)).
  • The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP- glucose, GDP-glucose) but is strictly specific for glucose.
  • The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor.
  • The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate.
  • This enzyme catalyzes the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria.
 1 A0A1C0U976
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