Reviewed,
UniProtKB/Swiss-Prot P07103 (GUNZ_DICD3)
Last modified
June 16, 2009.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Endoglucanase Z EC=3.2.1.4 Alternative name(s): Endo-1,4-beta-glucanase Z Short name=EGZ Cellulase Z | ||||
| Gene names |
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| Organism | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) | ||||
| Taxonomic identifier | 198628 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya |
Protein attributes
| Sequence length | 426 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Represents 97% of the global cellulase activity. |
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 5 (cellulase A) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | carbohydrate binding Inferred from electronic annotation. Source: InterPro cation bindingInferred from electronic annotation. Source: InterPro cellulase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||
Molecule processing | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 43 | 43 | |||||||||||||||||||
| Chain | 44 – 426 | 383 | Endoglucanase Z | PRO_0000007860 | |||||||||||||||||
Regions | |||||||||||||||||||||
| Region | 44 – 332 | 289 | Catalytic | ||||||||||||||||||
| Region | 333 – 366 | 34 | Linker | ||||||||||||||||||
| Region | 367 – 426 | 60 | Cellulose-binding | ||||||||||||||||||
Sites | |||||||||||||||||||||
| Active site | 176 | 1 | Proton donor | ||||||||||||||||||
| Active site | 263 | 1 | Nucleophile By similarity | ||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||
| Disulfide bond | 368 ↔ 425 | Ref.2 | |||||||||||||||||||
Experimental info | |||||||||||||||||||||
| Mutagenesis | 141 | 1 | H → A: Loss of activity. | ||||||||||||||||||
| Mutagenesis | 176 | 1 | E → A: Loss of activity. | ||||||||||||||||||
| Sequence conflict | 293 – 295 | 3 | SNA → QLTQ in CAA68604. Ref.1 | ||||||||||||||||||
| Sequence conflict | 350 – 364 | 15 | TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604. Ref.1 | ||||||||||||||||||
| Sequence conflict | 388 – 426 | 39 | THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN Ref.1 | ||||||||||||||||||
Secondary structure | |||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||
| Beta strand | 367 – 371 | 5 | |||||||||||||||||||
| Beta strand | 378 – 385 | 8 | |||||||||||||||||||
| Beta strand | 389 – 392 | 4 | |||||||||||||||||||
| Beta strand | 395 – 398 | 4 | |||||||||||||||||||
| Beta strand | 401 – 409 | 9 | |||||||||||||||||||
| Beta strand | 419 – 424 | 6 | |||||||||||||||||||
Sequences
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References
| [1] | "Homology between endoglucanase Z of Erwinia chrysanthemi and endoglucanases of Bacillus subtilis and alkalophilic Bacillus." Guiseppi A., Cami B., Aymeric J.-L., Ball G., Creuzet N. Mol. Microbiol. 2:159-164(1988) [PubMed: 2835589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi." Bortoli-German I., Brun E., Py B., Chippaux M., Barras F. Mol. Microbiol. 11:545-553(1994) [PubMed: 8152378] [Abstract] Cited for: SEQUENCE REVISION, DISULFIDE BOND. |
| [3] | "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis." Py B., Bortoli-German I., Haiech J., Chippaux M., Barras F. Protein Eng. 4:325-333(1991) [PubMed: 1677466] [Abstract] Cited for: MUTAGENESIS, DOMAINS. |
| [4] | "Stereochemistry of the hydrolysis reaction catalyzed by endoglucanase Z from Erwinia chrysanthemi." Barras F., Bortoli-German I., Bauzan M., Rouvier J., Gey C., Heyraud A., Henrissat B. FEBS Lett. 300:145-148(1992) [PubMed: 1563515] [Abstract] Cited for: STEREOCHEMISTRY OF THE REACTION. |
| [5] | "Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi." Brun E., Moriaud F., Gans P., Blackledge M.J., Barras F., Marion D. Biochemistry 36:16074-16086(1997) [PubMed: 9405041] [Abstract] Cited for: STRUCTURE BY NMR OF 365-426. |
| [6] | "Type II protein secretion in Gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi." Chapon V., Czjzek M., El Hassouni M., Py B., Juy M., Barras F. J. Mol. Biol. 310:1055-1066(2001) [PubMed: 11501995] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 44-335. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Y00540 Genomic DNA. Translation: CAA68604.1. | |||||||||||||||||||
| PIR | S03767. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| CAZy | CBM5. Carbohydrate-Binding Module Family 5. GH5. Glycoside Hydrolase Family 5. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003610. CBM_5_12. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. | ||||||||||||||||||
| Pfam | PF02839. CBM_5_12. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00495. ChtBD3. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | GUNZ_DICD3 | ||||||||
| Accession | Primary (citable) accession number: P07103 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


