PROSITE documentation PDOC00563

Glycosyl hydrolases family 6 signatures

Description

The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8) [1,2]. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family B [3] or as the glycosyl hydrolases family 6 [4,E1]. The enzymes which are currently known to belong to this family are listed below.

  • Agaricus bisporus exoglucanase 3 (cel3).
  • Cellulomonas fimi endoglucanase A (cenA).
  • Cellulomonas fimi exoglucanase A (cbhA).
  • Microspora bispora endoglucanase A (celA).
  • Streptomyces halstedii endoglucanases A (celA1).
  • Streptomyces strain KSM-9 endoglucanase 1 (casA).
  • Thermomonospora fusca endoglucanase E-2 (celB).
  • Trichoderma reesei exoglucanase II (CBH2).

One of the conserved regions in these enzymes contains a conserved aspartic acid residue which is potentially involved [5] in the catalytic mechanism; the aspartate is followed by a cysteine which is involved in a disulfide bond [6]. A second conserved region contains an aspartate which seems [5] to be the proton donor in the catalytic mechanism. We have used both regions as signature patterns.

Expert(s) to contact by email:

Henrissat B.

Last update:

May 2004 / Text revised.

Technical section

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

GLYCOSYL_HYDROL_F6_1, PS00655Glycosyl hydrolases family 6 signature 1  (PATTERN)
Consensus pattern: V-x-Y-x(2)-P-x-R-D-C-[GSAF]-x(2)-[GSA](2)-x-G
D may be an active site residue; C is involved in a disulfide bond
Sequences known to belong to this class detected by the pattern: ALL, except for celA1
Other sequence(s) detected in Swiss-Prot: NONE.
• 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 PS00655
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00655
Scan Swiss-Prot/TrEMBL entries against PS00655
view ligand binding statistics
Matching PDB structures: 1BVW 1GZ1 1HGY 1OC5 ... [ALL]
GLYCOSYL_HYDROL_F6_2, PS00656Glycosyl hydrolases family 6 signature 2  (PATTERN)
Consensus pattern: [LIVMYA]-[LIVA]-[LIVT]-[LIV]-E-P-D-[SAL]-[LI]-[PSAG]
D is an active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• 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 PS00656
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00656
Scan Swiss-Prot/TrEMBL entries against PS00656
view ligand binding statistics
Matching PDB structures: 1BVW 1CB2 1DYS 1GZ1 ... [ALL]

References

1 Authors Beguin P.
Title Molecular biology of cellulose degradation.
Source Annu. Rev. Microbiol. 44:219-248(1990).
PubMed ID 2252383
DOI 10.1146/annurev.mi.44.100190.001251
2 Authors Gilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
Title Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Source Microbiol. Rev. 55:303-315(1991).
PubMed ID 1886523
3 Authors Henrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J.-P.
Title Cellulase families revealed by hydrophobic cluster analysis.
Source Gene 81:83-95(1989).
PubMed ID 2806912
4 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
5 Authors Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K., Jones T.A.
Title Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.
Source Science 249:380-386(1990).
PubMed ID 2377893
6 Authors Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
Title Structural and functional relationships in two families of beta-1,4-glycanases.
Source Eur. J. Biochem. 202:367-377(1991).
PubMed ID 1761039
E1
Source http://www.uniprot.org/docs/glycosid

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