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It has been shown [1,2,3,4] that the following glycosyl hydrolases can be, on the basis of sequence similarities, classified into a single family:

• β-glucosidases (EC 3.2.1.21) from various bacteria such as Agrobacterium strain ATCC 21400, Bacillus polymyxa, and Caldocellum saccharolyticum.
• Two plants (clover) β-glucosidases (EC 3.2.1.21).
• Two different β-galactosidases (EC 3.2.1.23) from the archaebacteria Sulfolobus solfataricus (genes bgaS and lacS).
• 6-phospho-β-galactosidases (EC 3.2.1.85) from various bacteria such as Lactobacillus casei, Lactococcus lactis, and Staphylococcus aureus.
• 6-phospho-β-glucosidases (EC 3.2.1.86) from Escherichia coli (genes bglB and ascB) and from Erwinia chrysanthemi (gene arbB).
• Plants myrosinases (EC 3.2.1.147) (sinigrinase) (thioglucosidase).
• Mammalian lactase-phlorizin hydrolase (LPH) (EC 3.2.1.108 / EC 3.2.1.62). LPH, an integral membrane glycoprotein, is the enzyme that splits lactose in the small intestine. LPH is a large protein of about 1900 residues which contains four tandem repeats of a domain of about 450 residues which is evolutionary related to the above glycosyl hydrolases.

One of the conserved regions in these enzymes is centered on a conserved glutamic acid residue which has been shown [5], in the β-glucosidase from Agrobacterium, to be directly involved in glycosidic bond cleavage by acting as a nucleophile. We have used this region as a signature pattern. As a second signature pattern we selected a conserved region, found in the N-terminal extremity of these enzymes, this region also contains a glutamic acid residue.

This pattern will pick up the last two domains of LPH; the first two domains, which are removed from the LPH precursor by proteolytic processing, have lost the active site glutamate and may therefore be inactive [4].

F-x-[FYWM]-[GSTA]-x-[GSTA]-x-[GSTA](2)-[FYNH]-[NQ]-x-E-x- [GSTA]

ALL.

NONE.

This pattern will pick up the last three domains of LPH.

Henrissat B.

November 1995 / Patterns and text revised.

PROSITE methods (with tools and information) covered by this documentation:

GLYCOSYL_HYDROL_F1_1, PS00572; Glycosyl hydrolases family 1 active site  (PATTERN)

Consensus pattern: [LIVMFSTC]-[LIVFYS]-[LIV]-[LIVMST]-E-N-G-[LIVMFAR]-[CSAGN] E is the active site residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: 14.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00572 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00572 • Scan Swiss-Prot/TrEMBL entries against PS00572 • view ligand binding statistics

Matching PDB structures: 1BGA 1BGG 1CBG 1DWA ... [ALL]

GLYCOSYL_HYDROL_F1_2, PS00653; Glycosyl hydrolases family 1 N-terminal signature  (PATTERN)

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00653 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00653 • Scan Swiss-Prot/TrEMBL entries against PS00653 • view ligand binding statistics

Matching PDB structures: 1BGA 1BGG 1CBG 1DWA ... [ALL]

1	Authors	Henrissat B.
	Title	A classification of glycosyl hydrolases based on amino acid sequence similarities.
	Source	Biochem. J. 280:309-316(1991).
	PubMed ID	1747104

2	Authors	Henrissat B.
	Title	Sequence homology between a beta-galactosidase and some beta-glucosidases.
	Source	Protein Seq. Data Anal. 4:61-62(1991).
	PubMed ID	1924272

3	Authors	Gonzalez-Candelas L., Ramon D., Polaina J.
	Source	Gene 95:31-38(1990).

4	Authors	El Hassouni M., Henrissat B., Chippaux M., Barras F.
	Source	J. Bacteriol. 174:765-777(1992).

5	Authors	Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B., Aebersold R.
	Source	J. Am. Chem. Soc. 112:5887-5889(1990).

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