Literature summary for 3.13.1.1 extracted from

Meyer, B.H.; Zolghadr, B.; Peyfoon, E.; Pabst, M.; Panico, M.; Morris, H.R.; Haslam, S.M.; Messner, P.; Schaeffer, C.; Dell, A.; Albers, S.V.
Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius (2011), Mol. Microbiol., 82, 1150-1163.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sulfolobus acidocaldarius
gene agl3, DNA sequencing and analysis of gene agl3 as part of a gene cluster involved in the biosynthesis of sulfoquinovose and important for the assembly of the S-layer N-glycans, expression in Sulfolobus solfataricus agl3 deletion mutant under the control of a maltose inducible promoter using vector pSVA1450, the expression of agl3 leads to the restoration of the production of full-length glycan	Sulfolobus acidocaldarius

Cloned (Comment)

Organism

expression in Escherichia coli

Sulfolobus acidocaldarius

gene agl3, DNA sequencing and analysis of gene agl3 as part of a gene cluster involved in the biosynthesis of sulfoquinovose and important for the assembly of the S-layer N-glycans, expression in Sulfolobus solfataricus agl3 deletion mutant under the control of a maltose inducible promoter using vector pSVA1450, the expression of agl3 leads to the restoration of the production of full-length glycan

Sulfolobus acidocaldarius

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions	Sulfolobus acidocaldarius

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
UDP-alpha-D-glucose + sulfite	Sulfolobus acidocaldarius	-	UDP-alpha-D-sulfoquinovopyranose + H2O	-	?
UDP-alpha-D-glucose + sulfite	Sulfolobus acidocaldarius	the enzyme plays an important role in building up the glycans, which are attached to the S-layer and the flagellin proteins	UDP-alpha-D-sulfoquinovopyranose + H2O	-	?
UDP-alpha-D-glucose + sulfite	Sulfolobus acidocaldarius MW001	-	UDP-alpha-D-sulfoquinovopyranose + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Sulfolobus acidocaldarius	-	gene agl3, or Saci0423, of the sulfoquinovose biosynthesis operon	-
Sulfolobus acidocaldarius	Q4JBJ3	-	-
Sulfolobus acidocaldarius MW001	-	gene agl3, or Saci0423, of the sulfoquinovose biosynthesis operon	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sulfolobus acidocaldarius

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
UDP-alpha-D-glucose + sulfite	-	Sulfolobus acidocaldarius	UDP-alpha-D-sulfoquinovopyranose + H2O	-	?
UDP-alpha-D-glucose + sulfite	the enzyme plays an important role in building up the glycans, which are attached to the S-layer and the flagellin proteins	Sulfolobus acidocaldarius	UDP-alpha-D-sulfoquinovopyranose + H2O	-	?
UDP-alpha-D-glucose + sulfite	-	Sulfolobus acidocaldarius MW001	UDP-alpha-D-sulfoquinovopyranose + H2O	-	?

Synonyms

Synonyms	Comment	Organism
Agl3	-	Sulfolobus acidocaldarius
Saci_0423	-	Sulfolobus acidocaldarius

General Information

General Information	Comment	Organism
malfunction	in-frame deletion of agl3 results in a decreased molecular mass of the S-layer glycoprotein SlaA and the flagellin FlaB, indicating a change in the N-glycan composition with reduced trisaccharide structure composed of Man1GlcNAc2, missing the sulfoquinovose, a mannose and glucose. Cells lacking agl3 had a significantly lower growth rate at elevated salt concentrations compared with the background strain, overview	Sulfolobus acidocaldarius
metabolism	the enzyme is critical for biosynthesis of UDP-sulfoquinovose	Sulfolobus acidocaldarius