Glycoside Hydrolase Family 8

Known Activitieschitosanase (EC 3.2.1.132); cellulase (EC 3.2.1.4); licheninase (EC 3.2.1.73); endo-1,4-β-xylanase (EC 3.2.1.8); reducing-end-xylose releasing exo-oligoxylanase (EC 3.2.1.156)
Mechanism Inverting
ClanGH-M
3D Structure Status( α / α ) 6
Catalytic Nucleophile/BaseAsp (inferred)
Catalytic Proton DonorGlu (experimental)
Noteformerly known as cellulase family D
External resourcesCAZypedia; InterPro; PFAM; PRINTS; PROSITE;
Commercial Enzyme Provider(s)NZYTech; PROZOMIX;
Statistics GenBank accession (607); Uniprot accession (348); PDB accession (26); 3D entries (8); cryst (1)
All (537) Bacteria (526) Eukaryota (1) unclassified (10) Structure (8 - 1 cryst) Characterized (55)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 endoglucanase (CelY;Aq_1401) (Cel8Y) 3.2.1.4 Aquifex aeolicus VF5 AAC07361.1
NP_213966.1
O67401  
 chitosanase (BC2682) 3.2.1.132 Bacillus cereus ATCC 14579 AAP09638.1
NP_832437.1
Q81CR5  
 chitosanase (fragment) 3.2.1.132 Bacillus cereus D-11      
 chitosanase (ChoA) 3.2.1.132 Bacillus cereus H-1 AAO49750.1 Q849S1  
 chitosanase (Csn) 3.2.1.132 Bacillus cereus KNUC51 AAQ19678.1 Q6WCD7  
 chitosanase (Csn) 3.2.1.132 Bacillus cereus KNUC55 AAQ75086.1 Q6JUT6  
 endoglucanase N257 (Egl257) 3.2.1.4 Bacillus circulans KSM N257 BAB69035.1 Q93HV0  
 chitosanase / lichenase (Bgc) 3.2.1.132
3.2.1.73
Bacillus circulans WL-12 CAA37062.1 P19254.1  
 reducing-end-xylose releasing exo-oligoxylanase (Rex;BH2105) 3.2.1.156 Bacillus halodurans C-125 BAB05824.1
NP_242971.1
Q9KB30 1WU4[A]
1WU5[A]
1WU6[A]
2DRO[A]
2DRQ[A]
2DRR[A]
2DRS[A]
3A3V[A]
 endo-1,4-glucanase 3.2.1.4 Bacillus sp. AAA22409.1 P29019.1  
 chitosanase (ChoK) 3.2.1.132 Bacillus sp. K17     1V5C[A]
1V5D[A,B]
 chitosanase (Csn45) 3.2.1.132 Bacillus sp. KCTC 0377BP AAK07481.1 Q9ALZ1  
 xylanase Y (XylY) 3.2.1.8 Bacillus sp. KK-1 AAC27700.1 O52730  
 chitosanase 3.2.1.132 Bacillus sp. MET 1299      
 chitosanase 3.2.1.132 Bacillus sp. No.7-M BAB19277.1 Q9F1P1  
 chitosanase 3.2.1.132 Bacillus sp. S65      
 chitosanase (Cho-GG) 3.2.1.132 Bacillus thuringiensis JAM-GG01 BAJ05248.1 D4QGQ4  
 chitosanase (BTC11) 3.2.1.132 Bacillus thuringiensis serovar alesti ABO61887.1 A9P7F5  
 chitosanase (BTC19) 3.2.1.132 Bacillus thuringiensis serovar canadensis ABO61894.1 A9P7G2  
 chitosanase (BTC36) 3.2.1.132 Bacillus thuringiensis serovar darmstadiensis ABO61891.1 A9P7F9  
 chitosanase (BTC42) 3.2.1.132 Bacillus thuringiensis serovar israelensis ABO61892.1 A9P7G0  
 chitosanase (BTC30) 3.2.1.132 Bacillus thuringiensis serovar morrisoni ABO61890.1 A9P7F8  
 chitosanase (BTC31) 3.2.1.132 Bacillus thuringiensis serovar san diego ABO61888.1 A9P7F6  
 chitosanase (BTC13) 3.2.1.132 Bacillus thuringiensis serovar sotto ABO61893.1 A9P7G1  
 chitosanase (BTC40) 3.2.1.132 Bacillus thuringiensis serovar thompsoni ABO61889.1 A9P7F7  
 chitosanase (BTC50) 3.2.1.132 Bacillus thuringiensis serovar tochigiensis ABO61895.1 A9P7G3  
 reducing end xylose-releasing exo-oligoxylanase (RexA;BAD_0300) 3.2.1.156 Bifidobacterium adolescentis ATCC 15703 BAF39081.1 A1A048  
 reducing end xylose-releasing exo-oligoxylanase (RexA;XylA) 3.2.1.156 Bifidobacterium adolescentis DSM 20083 AAO67498.1 Q5JB57  
 endo-β-1,4-glucanase (fragment) 3.2.1.4 Cellulomonas uda CB4 AAA23090.1 P18336.1  
 endo-β-1,4-glucanase C (CelC;Ccel_0730) (Cel8C) 3.2.1.4 Clostridium cellulolyticum H10 ATCC 35319 AAA73867.1
ACL75109.1
P37699 1G4L
1G4N
 endo-β-1,4-glucanase B (CelB) (Cel8A) 3.2.1.4 Clostridium josui BAA04078.1
BAI52925.1
D1MX94
P37701
 
 endo-β-1,4-glucanase A (CelA;Cthe_0269) (Cel8A) 3.2.1.4 Clostridium thermocellum ATCC 27405 ABN51508.1 A3DC29  
 endo-β-1,4-glucanase A (CelA) (Cel8A) 3.2.1.4 Clostridium thermocellum NCIB 10682 / JW20 AAA83521.1 P04955 1CEM[A]
1IS9[A]
1KWF[A]
 endo-β-1,4-glucanase Y (CelY) 3.2.1.4 Dickeya dadantii 3937 AAA24818.1
ADM96331.1
P27032.1  
 endoglucanase 3.2.1.4 Enterobacter cloacae JV ACU11859.1 C7FFS4  
 endoglucanase 8Y (Cel8Y) 3.2.1.4 Erwinia chrysanthemi PY35 AAG49556.1 Q9APJ5  
 endoglucanase (CelA) 3.2.1.4 Erwinia rhapontici NCPPB2989 CAB89803.1 Q9L3G9  
 endo-β-1,4-glucanase (YhjM;BcsC;b3531) (periplasmic) 3.2.1.4 Escherichia coli K-12 MG1655 AAB18508.1
AAC76556.1
NP_417988.1
P37651 3QXF[A,B,C,D]
3QXQ[A,B,C,D]
 endoglucanase (Fisuc_1802;FSU_2303) (Cel8B) 3.2.1.4 Fibrobacter succinogenes subsp. succinogenes S85 ABU45499.1
ACX75395.1
ADL24942.1
A7UG68  
 endo-β-1,4-glucanase (CMCax;AEG) 3.2.1.4 Gluconacetobacter xylinus ATCC 23769 AAA16969.1 P37696 1WZZ[A]
 endo-β-1,4-glucanase (CMCax;CMCase;Orf1) 3.2.1.4 Gluconacetobacter xylinus BPR2001 AAQ38000.1
BAA31461.1
O82857  
 endo-β-1,4-glucanase (Cel8H) 3.2.1.4 Halomonas sp. 1339 ACN29537.1    
 cellulase 3.2.1.4 Jeongeupia naejangsanensis Njc02 ADN52626.1 E2G4E3  
 endo-β-1,4-glucanase (CMCase) 3.2.1.4 Klebsiella pneumoniae SC ACO70964.1 C9WB00  
 bifunctional endoglucanase chitosanase (Cel8A) 3.2.1.132
3.2.1.4
Lysobacter sp. IB-9374 BAE86850.1 Q25C15  
 chitosanase-glucanase 3.2.1.132
3.2.1.4
3.2.1.73
Paenibacillus fukuinensis D2 BAB64835.1 Q93IE7  
 endo-β-1,4-xylanase (Xyn8) 3.2.1.8 Pseudoalteromonas arctica CBY88881.1    
 endo-β-1,4-xylanase (Xyl;XPH) 3.2.1.8 Pseudoalteromonas haloplanktis TAH3A CAD20872.1
CAJ30796.1
CAJ33706.1
Q8RJN8 1H12[A]
1H13[A]
1H14[A]
1XW2[A]
1XWQ[A]
1XWT[A]
2A8Z[A]
2B4F[A]
 cellulase C2 (Celc2) 3.2.1.4 Rhizobium leguminosarum bv. trifolii ANU843 CAD90973.1 Q83XK5  
 endoglucanase (BcsZ) 3.2.1.4 Salmonella typhimurium ATCC14028 CAC44017.1 Q8ZLB7  
 endoglucanase (BcsC;BcsZ;STM3617) 3.2.1.4 Salmonella typhimurium LT2 SGSC 1412; ATCC 700720 AAL22477.1
CAC86197.1
NP_462518.1
Q8ZLB7  
 endoglucanase (CelC;CMCase) 3.2.1.4 Salmonella typhimurium UR1 AAL69395.1
AAO33380.1
Q7B8Q5
Q8ZLB7
 
 endo-β-1,4-xylanase (XYL6806) 3.2.1.8 uncultured bacterium AAS85781.1 Q6QHA3  
 xylanase (Xyn8) (Xyn8) 3.2.1.8 uncultured bacterium ABB71891.1 Q0H3C1 cryst
 endoglucanase (CelA;ZMO1086) 3.2.1.4 Zymomonas mobilis subsp. mobilis ZM4 AAV89710.1    

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.





Last update: 2012-01-31 © Copyright 1998-2012
AFMB - CNRS - Universités Aix-Marseille I & II