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:

"
HAD superfamily/HAD-like
".

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 37: D,D-heptose 1,7-bisphosphate phosphatase

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
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase. [EC: 3.1.3.82]
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(2)O = D-glycero-beta- D-manno-heptose 1-phosphate + phosphate.
  • The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno- heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria.
  • In vitro the catalytic efficiency with the beta-anomer is 100-200- fold higher than with the alpha-anomer.
6192 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22 A0A027ZG22
(6182 more...)
D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase. [EC: 3.1.3.83]
D-glycero-alpha-D-manno-heptose-1,7-bisphosphate + H(2)O = D-glycero- alpha-D-manno-heptose-1-phosphate + phosphate.
  • The enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D- manno-heptose, which is required for assembly of S-layer glycoprotein in some Gram-positive bacteria.
  • The in vitro catalytic efficiency of the enzyme from Bacteroides thetaiotaomicron is 6-fold higher with the alpha-anomer than with the beta-anomer.
69 A0A0E1U218 A0A0E1U218 A0A0E1U218 A0A0E1U218 A0A0E1U218 A0A0E1U218 A0A0E1U218 A0A0E1U218 A0A0F6GCE9 A0A0F6GCE9
(59 more...)