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Enzyme Name | UniProtKB | KEGG |
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| P26222 |
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Protein name | Endoglucanase E-2 | cellulaseendo-1,4-beta-D-glucanasebeta-1,4-glucanasebeta-1,4-endoglucan hydrolasecelluase Acellulosin APendoglucanase Dalkali cellulasecellulase A 3celludextrinase9.5 cellulaseavicelasepancellase SS1,4-(1,31,4)-beta-D-glucan 4-glucanohydrolase |
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Synonyms | EC 3.2.1.4Endo-1,4-beta-glucanase E-2Cellulase E-2Cellulase E2 |
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Pfam | PF00553 (CBM_2) PF01341 (Glyco_hydro_6) [Graphical view]
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CAZy | GH6 (Glycoside Hydrolase Family)
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KEGG pathways | MAP code | Pathways |
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MAP00500 | Starch and sucrose metabolism |
UniProtKB:Accession Number | P26222 |
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Entry name | GUN2_THEFU |
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Activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
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Subunit | Homodimer. |
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Subcellular location |
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Cofactor |
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Active-site residues | resource |
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Swiss-prot;P26222 | pdb | Catalytic residues |
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| | | | | | | | |
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1tmlA |  |  |  |  |  |  |  | ASP 79;ASP 117;ASP 156;ASP 265
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[10] | p.9750-9751 |
| [11] | p.204-206 |
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references | [1] |
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PubMed ID | 8215374 |
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Journal | Appl Environ Microbiol |
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Year | 1993 |
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Volume | 59 |
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Pages | 3032-43 |
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Authors | Jung ED, Lao G, Irwin D, Barr BK, Benjamin A, Wilson DB |
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Title | DNA sequences and expression in Streptomyces lividans of an exoglucanase gene and an endoglucanase gene from Thermomonospora fusca. |
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[2] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317. |
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Medline ID | 94002001 |
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PubMed ID | 8399160 |
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Journal | Biochemistry |
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Year | 1993 |
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Volume | 32 |
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Pages | 9906-16 |
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Authors | Spezio M, Wilson DB, Karplus PA |
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Title | Crystal structure of the catalytic domain of a thermophilic endocellulase. |
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Related PDB | 1tml |
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Related UniProtKB | P26222 |
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[3] |
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PubMed ID | 7789807 |
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Journal | Gene |
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Year | 1995 |
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Volume | 158 |
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Pages | 23-9 |
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Authors | Quillet L, Barray S, Labedan B, Petit F, Guespin-Michel J |
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Title | The gene encoding the beta-1,4-endoglucanase (CelA) from Myxococcus xanthus: evidence for independent acquisition by horizontal transfer of binding and catalytic domains from actinomycetes. |
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[4] |
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PubMed ID | 8615816 |
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Journal | Biochem J |
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Year | 1996 |
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Volume | 315 |
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Pages | 467-72 |
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Authors | Damude HG, Ferro V, Withers SG, Warren RA |
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Title | Substrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6. |
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[5] |
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PubMed ID | 8824619 |
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Journal | J Bacteriol |
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Year | 1996 |
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Volume | 178 |
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Pages | 5732-40 |
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Authors | Ahsan MM, Kimura T, Karita S, Sakka K, Ohmiya K |
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Title | Cloning, DNA sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome. |
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[6] |
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PubMed ID | 9438981 |
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Journal | Biosci Biotechnol Biochem |
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Year | 1997 |
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Volume | 61 |
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Pages | 2004-9 |
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Authors | Hitomi J, Hatada Y, Kawaminami S, Kawai S, Ito S |
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Title | Amino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain. |
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[7] |
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PubMed ID | 9335169 |
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Journal | J Biotechnol |
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Year | 1997 |
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Volume | 57 |
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Pages | 101-13 |
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Authors | Zhang S, Wilson DB |
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Title | Surface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2. |
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[8] |
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PubMed ID | 9649302 |
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Journal | Biochemistry |
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Year | 1998 |
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Volume | 37 |
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Pages | 9220-9 |
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Authors | Barr BK, Wolfgang DE, Piens K, Claeyssens M, Wilson DB |
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Title | Active-site binding of glycosides by Thermomonospora fusca endocellulase E2. |
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[9] |
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PubMed ID | 10029552 |
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Journal | Biochemistry |
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Year | 1999 |
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Volume | 38 |
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Pages | 2570-6 |
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Authors | Beadle BM, Baase WA, Wilson DB, Gilkes NR, Shoichet BK |
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Title | Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme. |
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[10] |
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PubMed ID | 10423254 |
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Journal | Biochemistry |
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Year | 1999 |
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Volume | 38 |
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Pages | 9746-51 |
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Authors | Wolfgang DE, Wilson DB |
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Title | Mechanistic studies of active site mutants of Thermomonospora fusca endocellulase E2. |
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[11] |
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Comments | X-ray crystallography |
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PubMed ID | 10794732 |
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Journal | Biochem J |
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Year | 2000 |
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Volume | 348 Pt 1 |
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Pages | 201-7 |
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Authors | Davies GJ, Brzozowski AM, Dauter M, Varrot A, Schulein M |
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Title | Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution. |
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Related PDB | 1dys |
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[12] |
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PubMed ID | 10731432 |
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Journal | J Mol Biol |
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Year | 2000 |
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Volume | 297 |
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Pages | 819-28 |
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Authors | Varrot A, Schulein M, Davies GJ |
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Title | Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form. |
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[13] |
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PubMed ID | 11311718 |
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Journal | Int J Biol Macromol |
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Year | 2001 |
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Volume | 28 |
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Pages | 285-92 |
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Authors | Novo C, Simoes F, Mendonca D, Matos J, Clemente A |
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Title | Primary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor. |
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[14] |
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PubMed ID | 11514516 |
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Journal | J Bacteriol |
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Year | 2001 |
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Volume | 183 |
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Pages | 5325-33 |
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Authors | Steenbakkers PJ, Li XL, Ximenes EA, Arts JG, Chen H, Ljungdahl LG, Op Den Camp HJ |
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Title | Noncatalytic docking domains of cellulosomes of anaerobic fungi. |
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[15] |
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PubMed ID | 11495244 |
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Journal | J Biomol NMR |
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Year | 2001 |
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Volume | 20 |
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Pages | 127-33 |
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Authors | Permi P, Annila A |
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Title | A new approach for obtaining sequential assignment of large proteins. |
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[16] |
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PubMed ID | 12071852 |
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Journal | Biochem J |
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Year | 2002 |
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Volume | 365 |
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Pages | 193-204 |
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Authors | Steenbakkers PJ, Ubhayasekera W, Goossen HJ, van Lierop EM, van der Drift C, Vogels GD, Mowbray SL, Op den Camp HJ |
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Title | An intron-containing glycoside hydrolase family 9 cellulase gene encodes the dominant 90 kDa component of the cellulosome of the anaerobic fungus Piromyces sp. strain E2. |
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comments | The catalytic domain of this enzyme homologous to the counterpart enzyme from Humicola insolens (S00194 in EzCatDB). This family belongs to Glycosidase family-6, which has an inverting mechanism (equatorial to axial conformation). Furthermore, this enzyme belongs to endoglucanase, whilst its family member (EC 3.2.1.91) is exoglucanase. According to the Swiss-prot (P26222), Asp117 acts as proton donor, whilst Asp265 acts as base. The rest of aspartic residues serve as pKa modulator. However, literature [10] suggests that the residue corresponding to Asp265 plays an important role in binding rather than as base. In contrast, [11] suggests that the possiblity of Asp265 as base catalyst could not be ruled out.
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created | updated |
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2002-10-15 | 2009-03-24 |
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