CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family Sulfotransferase

Enzyme Information

2.8.2.30
[Heparan sulfate]-glucosamine 3-sulfotransferase 3.
based on mapping to UniProt Q9Y663
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).

UniProtKB Entries (1)

Q9Y663
HS3SA_HUMAN
Homo sapiens
Heparan sulfate glucosamine 3-O-sulfotransferase 3A1

PDB Structure

PDB 1T8U
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1
Moon, A.F., Edavettal, S.C., Krahn, J.M., Munoz, E.M., Negishi, M., Linhardt, R.J., Liu, J., Pedersen, L.C.
J.Biol.Chem.
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