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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 623830: Heparan sulfate glucosamine 3-O-sulfotransferase 5

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
[Heparan sulfate]-glucosamine 3-sulfotransferase 1. [EC: 2.8.2.23]
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
  • This enzyme differs from EC 2.8.2.29 and EC 2.8.2.30 by being the most selective for a precursor of the antithrombin-binding site.
  • It has a minimal acceptor sequence of: -> GlcNAc6S->GlcA-> GlcN2S*+-6S->IdoA2S->GlcN2S->.
  • It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites.
  • These precursors are variants of the consensus sequence: -> Glc(N2S>NAc)+-6S->GlcA->GlcN2S*+-6S->GlcA>IdoA+-2S-> Glc(N2S/NAc)+-6S->.
  • If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA.
 17 A0A024R9R4 A2RTI7 B2RXW6 B7PP95 B7PRN4 E0VBB6 O14792 O35310 Q52KJ0 Q5GFD5
(7 more...)
[Heparan sulfate]-glucosamine 3-sulfotransferase 2. [EC: 2.8.2.29]
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
  • This enzyme sulfates the residues marked with an asterisk in sequences containing at least ->IdoA2S->GlcN*-> or ->GlcA2S->GlcN*->.
  • Preference for GlcN2S versus unmodified GlcN has not yet been established.
  • Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant.
  • This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 prefers GlcA or IdoA, whereas EC 2.8.2.30 prefers IdoA2S.
 4 G3SA34 Q673U1 Q80W66 Q9Y278
[Heparan sulfate]-glucosamine 3-sulfotransferase 3. [EC: 2.8.2.30]
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
  • Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN*-> and -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN6S*-> with modification of the N-unsubstituted glucosamine residue (shown with an asterisk).
  • Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded.
  • The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells.
  • There are two isozymes, known as 3-OST-3(A) and 3-OST-3(B), which have identical catalytic domains but are encoded by different mammalian genes.
  • The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases.
  • It is inefficient at modifying precursors of the antithrombin binding site (in contrast to EC 2.8.2.23) and it does not modify glucosamine preceded by GlcA2S (unlike EC 2.8.2.29).
 3 Q9QZS6 Q9Y662 Q9Y663
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