DB code: S00150
| RLCP classification | 1.30.36211.992 : Hydrolysis | |
|---|---|---|
| CATH domain | 2.60.120.180 : Jelly Rolls | Catalytic domain |
| E.C. | 3.2.1.4 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.60.120.180 : Jelly Rolls | S00533 S00151 D00504 D00538 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | CAZy | Pfam |
|---|---|---|---|---|
| O33897 |
|
Cellulase
EC 3.2.1.4 |
GH12
(Glycoside Hydrolase Family 12)
|
PF01670
(Glyco_hydro_12)
[Graphical View] |
| O00095 |
|
Endo-beta-1,4-glucanase (Beta-1,4-glucanase)
EC 3.2.1.4 |
GH12
(Glycoside Hydrolase Family 12)
|
PF01670
(Glyco_hydro_12)
[Graphical View] |
| Q8NJY3 |
|
Endoglucanase
|
GH12
(Glycoside Hydrolase Family 12)
|
PF01670
(Glyco_hydro_12)
[Graphical View] |
| Q8NJY6 |
|
Endoglucanase
|
GH12
(Glycoside Hydrolase Family 12)
|
PF01670
(Glyco_hydro_12)
[Graphical View] |
| KEGG enzyme name |
|---|
|
cellulase
endo-1,4-beta-D-glucanase beta-1,4-glucanase beta-1,4-endoglucan hydrolase celluase A cellulosin AP endoglucanase D alkali cellulase cellulase A 3 celludextrinase 9.5 cellulase avicelase pancellase SS 1,4-(1,3 1,4)-beta-D-glucan 4-glucanohydrolase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| O33897 | O33897_RHOMR | ||||
| O00095 | O00095_TRIRE | ||||
| Q8NJY3 | Q8NJY3_9ASCO | ||||
| Q8NJY6 | Q8NJY6_9HYPO |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00500 | Starch and sucrose metabolism |
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00760 | C00478 | C00551 | C00001 | C00760 | C00551 | |||||||
| E.C. | |||||||||||||
| Compound | Cellulose | Lichenin | beta-D-Glucan | H2O | Cellulose | beta-D-Glucan | Transition-state for glycosylated enzyme | Glycosylated enzyme intermediate | |||||
| Type | polysaccharide | carbohydrate | polysaccharide | H2O | polysaccharide | polysaccharide | |||||||
| ChEBI |
15377 15377 |
||||||||||||
| PubChem |
439241 439241 |
46173706 46173706 |
22247451 962 22247451 962 |
46173706 46173706 |
|||||||||
| 1h0bA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1h0bB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2bw8A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2bw8B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2bwaA |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:GLC-BGC-BGC | Unbound | |||
| 2bwaB |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:GLC-BGC | Unbound | |||
| 2bwcA |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:GLC-BGC-BGC | Unbound | |||
| 2bwcB |
|
|
|
|
|
Bound:GLC-BGC-BGC-BGC | Unbound | Unbound | Bound:BGC-BGC-BGC | Unbound | |||
| 1h8vA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1h8vB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1h8vC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1h8vD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1h8vE |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1h8vF |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa2A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa2B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa2C |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa2D |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa2E |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa2F |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1olqA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1olqB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1olrA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1uu4A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Bound:BGC-BGC | |||
| 1uu5A |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:BGC-BGC-BGC-BGC | Unbound | |||
| 1uu6A |
|
|
|
|
|
Bound:BGC-BGC-BGC-BGC | Unbound | Unbound | Unbound | Unbound | |||
| 1w2uA |
|
|
|
|
|
Bound:BGC-BGC-BGC-BGC | Unbound | Unbound | Unbound | Unbound | |||
| 1oa3A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa3B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa3C |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1oa3D |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [2], [3], [5], [7] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1h0bA |
|
|
|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 1h0bB |
|
|
|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 2bw8A |
|
|
|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 2bw8B |
|
|
|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 2bwaA |
|
|
|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 2bwaB |
|
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|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 2bwcA |
|
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|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 2bwcB |
|
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|
|
|
ASN 102;ASP 106;GLU 124;GLU 207 | ||||
| 1h8vA |
|
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|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1h8vB |
|
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|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1h8vC |
|
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|
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|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1h8vD |
|
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|
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|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1h8vE |
|
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|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1h8vF |
|
|
|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa2A |
|
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|
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|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa2B |
|
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|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa2C |
|
|
|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa2D |
|
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|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa2E |
|
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|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa2F |
|
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|
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|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1olqA |
|
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|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1olqB |
|
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|
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|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1olrA |
|
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|
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ASN 99;ASP 103;GLU 120;GLU 205 | ||||
| 1uu4A |
|
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ASN 99;ASP 103;GLU 120;GLU 205 | ||||
| 1uu5A |
|
|
|
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ASN 99;ASP 103;GLU 120;GLU 205 | ||||
| 1uu6A |
|
|
|
|
|
ASN 99;ASP 103;GLU 120;GLU 205 | ||||
| 1w2uA |
|
|
|
|
|
ASN 99;ASP 103;GLU 120;GLU 205 | ||||
| 1oa3A |
|
|
|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa3B |
|
|
|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa3C |
|
|
|
|
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ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| 1oa3D |
|
|
|
|
|
ASN 95;ASP 99;GLU 116;GLU 200 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
p.16037-16038 | |
|
[3]
|
Scheme 1, p.139-140 | |
|
[4]
|
p.301 | |
|
[6]
|
p.888-889 | |
|
[9]
|
p.1510-1511 | |
|
[11]
|
Fig.2, p.252-254 | |
|
[12]
|
p.63-64, p.67 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8477842 |
| Journal | FEBS Lett |
| Year | 1993 |
| Volume | 321 |
| Pages | 135-9 |
| Authors | Torronen A, Kubicek CP, Henrissat B |
| Title | Amino acid sequence similarities between low molecular weight endo-1,4-beta-xylanases and family H cellulases revealed by clustering analysis. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9440876 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 16032-9 |
| Authors | Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ |
| Title |
The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9806895 |
| Journal | Biochem J |
| Year | 1998 |
| Volume | 336 |
| Pages | 139-45 |
| Authors | Zechel DL, He S, Dupont C, Withers SG |
| Title | Identification of Glu-120 as the catalytic nucleophile in Streptomyces lividans endoglucanase celB. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-234. |
| Medline ID | |
| PubMed ID | 11327768 |
| Journal | J Mol Biol |
| Year | 2001 |
| Volume | 308 |
| Pages | 295-310 |
| Authors | Sandgren M, Shaw A, Ropp TH, Wu S, Bott R, Cameron AD, Stahlberg J, Mitchinson C, Jones TA |
| Title |
The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, |
| Related PDB | 1h8v |
| Related UniProtKB | O00095 |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12073090 |
| Journal | Curr Genet |
| Year | 2002 |
| Volume | 41 |
| Pages | 89-98 |
| Authors | Goedegebuur F, Fowler T, Phillips J, van der Kley P, van Solingen P, Dankmeyer L, Power SD |
| Title | Cloning and relational analysis of 15 novel fungal endoglucanases from family 12 glycosyl hydrolase. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-260. |
| Medline ID | |
| PubMed ID | 12095262 |
| Journal | J Mol Biol |
| Year | 2002 |
| Volume | 320 |
| Pages | 883-97 |
| Authors | Crennell SJ, Hreggvidsson GO, Nordberg Karlsson E |
| Title |
The structure of Rhodothermus marinus Cel12A, |
| Related PDB | 1h0b |
| Related UniProtKB | O33897 |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 17-234. |
| Medline ID | |
| PubMed ID | 14627738 |
| Journal | Protein Sci |
| Year | 2003 |
| Volume | 12 |
| Pages | 2782-93 |
| Authors | Sandgren M, Gualfetti PJ, Paech C, Paech S, Shaw A, Gross LS, Saldajeno M, Berglund GI, Jones TA, Mitchinson C |
| Title | The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability. |
| Related PDB | 1olr 1olq |
| Related UniProtKB | O00095 Q8NJY3 |
| [8] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 17-234. |
| Medline ID | |
| PubMed ID | 12649442 |
| Journal | Protein Sci |
| Year | 2003 |
| Volume | 12 |
| Pages | 848-60 |
| Authors | Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C |
| Title | Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability. |
| Related PDB | 1oa2 1oa3 |
| Related UniProtKB | O00095 |
| [9] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 31-254. |
| Medline ID | |
| PubMed ID | 15364577 |
| Journal | J Mol Biol |
| Year | 2004 |
| Volume | 342 |
| Pages | 1505-17 |
| Authors | Sandgren M, Berglund GI, Shaw A, Stahlberg J, Kenne L, Desmet T, Mitchinson C |
| Title | Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A. |
| Related PDB | 1uu4 1uu5 1uu6 1w2u |
| Related UniProtKB | Q8NJY3 Q8NJY6 |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15456402 |
| Journal | Biochem J |
| Year | 2005 |
| Volume | 385 |
| Pages | 581-8 |
| Authors | Huang Y, Krauss G, Cottaz S, Driguez H, Lipps G |
| Title | A highly acid-stable and thermostable endo-beta-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15950056 |
| Journal | Prog Biophys Mol Biol |
| Year | 2005 |
| Volume | 89 |
| Pages | 246-91 |
| Authors | Sandgren M, Stahlberg J, Mitchinson C |
| Title |
Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 16343530 |
| Journal | J Mol Biol |
| Year | 2006 |
| Volume | 356 |
| Pages | 57-71 |
| Authors | Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E |
| Title | Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A. |
| Related PDB | 2bw8 2bwa 2bwc |
| Related UniProtKB | |
| Comments |
|---|
|
This family belongs to glycosidase family-12, The catalytic domain of this enzyme is homologous to those of another cellulase (S00533 in EzCatDB) and beta-1,4-Glucanase (D00504 in EzCatDB), According to the literature [2], (1) Asn102 (of 1h0b) may modulate the activity of Glu207 as a acid-base. (2) Glu207 (of 1h0b) acts as a general acid to protonate the leaving oxygen atom, (3) pKa of Glu124 (of 1h0b), (4) Glu124 makes a nucleophilic attack on C1 atom of the transition state, (5) Glu207 acts as a general base to activate a water molecule. (6) The activated water makes a nucleophilic attack on the C1 atom of the intermediate. |
| Created | Updated |
|---|---|
| 2004-05-17 | 2009-02-26 |