Species | Bacteroides sp900555635 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900555635 | |||||||||||
CAZyme ID | MGYG000004899_02664 | |||||||||||
CAZy Family | GH5 | |||||||||||
CAZyme Description | Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 106163; End: 107593 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 161 | 444 | 1.2e-80 | 0.9891304347826086 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00150 | Cellulase | 1.40e-40 | 146 | 415 | 1 | 242 | Cellulase (glycosyl hydrolase family 5). |
COG2730 | BglC | 1.08e-21 | 114 | 409 | 29 | 321 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
cd14948 | BACON | 1.30e-17 | 24 | 107 | 1 | 83 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
pfam13004 | BACON | 4.19e-05 | 49 | 107 | 1 | 61 | Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain. |
pfam19190 | BACON_2 | 6.84e-05 | 24 | 109 | 1 | 91 | Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QBJ18101.1 | 1.11e-258 | 2 | 475 | 7 | 477 |
QMI79558.1 | 1.57e-258 | 2 | 475 | 7 | 477 |
QUT65254.1 | 5.03e-258 | 2 | 475 | 10 | 480 |
QUT33510.1 | 5.03e-258 | 2 | 475 | 10 | 480 |
QUT61941.1 | 9.07e-258 | 2 | 475 | 7 | 477 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6XRK_A | 5.41e-62 | 128 | 470 | 23 | 372 | GH5-4broad specificity endoglucanase from an uncultured bovine rumen ciliate [uncultured bovine rumen ciliate],6XRK_B GH5-4 broad specificity endoglucanase from an uncultured bovine rumen ciliate [uncultured bovine rumen ciliate] |
4IM4_A | 4.25e-55 | 132 | 466 | 10 | 332 | ChainA, Endoglucanase E [Acetivibrio thermocellus],4IM4_B Chain B, Endoglucanase E [Acetivibrio thermocellus],4IM4_C Chain C, Endoglucanase E [Acetivibrio thermocellus],4IM4_D Chain D, Endoglucanase E [Acetivibrio thermocellus],4IM4_E Chain E, Endoglucanase E [Acetivibrio thermocellus],4IM4_F Chain F, Endoglucanase E [Acetivibrio thermocellus] |
6WQP_A | 5.65e-52 | 126 | 467 | 13 | 354 | GH5-4broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQP_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQV_A GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_C GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_D GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis] |
3NDY_A | 6.28e-52 | 123 | 459 | 7 | 331 | Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans] |
4X0V_A | 3.08e-51 | 126 | 467 | 37 | 393 | Structureof a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_B Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_C Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_D Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_E Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_F Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_G Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32],4X0V_H Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 [Caldicellulosiruptor sp. F32] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P10477 | 5.20e-51 | 132 | 466 | 60 | 382 | Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2 |
A7LXT7 | 1.58e-50 | 14 | 443 | 31 | 473 | Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02653 PE=1 SV=1 |
P28623 | 1.04e-49 | 123 | 459 | 38 | 362 | Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2 |
P23660 | 3.07e-49 | 123 | 442 | 22 | 327 | Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1 |
P17901 | 2.53e-47 | 133 | 467 | 51 | 398 | Endoglucanase A OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.000000 | 0.000006 | 1.000070 | 0.000000 | 0.000000 | 0.000000 |
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