PROSITE documentation PDOC00511

Glycosyl hydrolases family 9 active sites 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 E [3] or as the glycosyl hydrolases family 9 [4,E1]. The enzymes which are currently known to belong to this family are listed below.

  • Butyrivibrio fibrisolvens cellodextrinase 1 (ced1).
  • Cellulomonas fimi endoglucanases B (cenB) and C (cenC).
  • Clostridium cellulolyticum endoglucanase G (celCCG).
  • Clostridium cellulovorans endoglucanase C (engC).
  • Clostridium stercoararium endoglucanase Z (avicelase I) (celZ).
  • Clostridium thermocellum endoglucanases D (celD), F (celF) and I (celI).
  • Fibrobacter succinogenes endoglucanase A (endA).
  • Pseudomonas fluorescens endoglucanase A (celA).
  • Streptomyces reticuli endoglucanase 1 (cel1).
  • Thermomonospora fusca endoglucanase E-4 (celD).
  • Dictyostelium discoideum spore germination specific endoglucanase 270-6. This slime mold enzyme may digest the spore cell wall during germination, to release the enclosed amoeba.
  • Endoglucanases from plants such as Avocado or French bean. In plants this enzyme may be involved the fruit ripening process.

Two of the most conserved regions in these enzymes are centered on conserved residues which have been shown [5,6], in the endoglucanase D from Cellulomonas thermocellum, to be important for the catalytic activity. The first region contains an active site histidine and the second region contains two catalytically important residues: an aspartate and a glutamate. We have used both regions as signature patterns.

Expert(s) to contact by email:

Henrissat B.

Last update:

November 1997 / Text revised.

Technical section:

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

GLYCOSYL_HYDROL_F9_1, PS00592Glycosyl hydrolases family 9 active sites signature 1  (PATTERN)
Consensus pattern: [STV]-x-[LIVMFY]-[STV]-x(2)-G-x-[NKR]-x(4)-[PLIVM]-H-x-R
H is an active site residue
Sequences known to belong to this class detected by the pattern: ALL, except for Cellulomonas fimi cenC and Streptomyces reticuli cel1
Other sequence(s) detected in Swiss-Prot: 2.
• 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 PS00592
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00592
Scan Swiss-Prot/TrEMBL entries against PS00592
view ligand binding statistics
Matching PDB structures: 1CLC 1G87 1GA2 1JS4 ... [ALL]
GLYCOSYL_HYDROL_F9_2, PS00698Glycosyl hydrolases family 9 active sites signature 2  (PATTERN)
Consensus pattern: [FYW]-x-D-x(4)-[FYW]-x(3)-E-x-[STA]-x(3)-N-[STA]
D and E are active site residues
Sequences known to belong to this class detected by the pattern: ALL, except for Fibrobacter succinogenes endA whose sequence seems to be incorrect
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 PS00698
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00698
Scan Swiss-Prot/TrEMBL entries against PS00698
view ligand binding statistics
Matching PDB structures: 1CLC 1G87 1GA2 1JS4 ... [ALL]

References:

1 AuthorsBeguin P.
TitleMolecular biology of cellulose degradation.
SourceAnnu. Rev. Microbiol. 44:219-248(1990).
PubMed ID2252383
DOI10.1146/annurev.mi.44.100190.001251
2 AuthorsGilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
TitleDomains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
SourceMicrobiol. Rev. 55:303-315(1991).
PubMed ID1886523
3 AuthorsHenrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J.-P.
TitleCellulase families revealed by hydrophobic cluster analysis.
SourceGene 81:83-95(1989).
PubMed ID2806912
4 AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104
5 AuthorsTomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M.
TitleIdentification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum.
SourceJ. Biol. Chem. 266:10313-10318(1991).
PubMed ID2037583
6 AuthorsTomme P., van Beeumen J., Claeyssens M.
TitleModification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.
SourceBiochem. J. 285:319-324(1992).
PubMed ID1637316
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?glycosid.txt

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