Species | W3P20-009 sp900766825 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; W3P20-009; W3P20-009; W3P20-009 sp900766825 | |||||||||||
CAZyme ID | MGYG000003423_02125 | |||||||||||
CAZy Family | GH5 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16762; End: 18306 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 158 | 455 | 5.3e-88 | 0.9891304347826086 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00150 | Cellulase | 1.15e-47 | 149 | 456 | 7 | 270 | Cellulase (glycosyl hydrolase family 5). |
COG2730 | BglC | 2.93e-23 | 127 | 469 | 40 | 374 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
cd14948 | BACON | 7.91e-10 | 37 | 120 | 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 | 9.57e-05 | 63 | 120 | 2 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALJ60576.1 | 1.45e-163 | 8 | 502 | 15 | 507 |
QUT88430.1 | 1.58e-160 | 28 | 502 | 109 | 593 |
ADY35478.1 | 4.38e-156 | 38 | 502 | 121 | 587 |
QRX62664.1 | 2.60e-151 | 39 | 502 | 39 | 508 |
ADD61911.1 | 1.18e-150 | 47 | 502 | 14 | 480 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6WQY_A | 2.47e-149 | 129 | 485 | 22 | 378 | ChainA, Cellulase [Phocaeicola salanitronis DSM 18170] |
4YHE_A | 9.07e-116 | 138 | 502 | 14 | 381 | NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHE_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a] |
4YHG_A | 7.25e-115 | 138 | 502 | 14 | 381 | NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHG_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a] |
2JEP_A | 1.90e-78 | 134 | 458 | 38 | 367 | Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli] |
3NDY_A | 8.15e-57 | 134 | 474 | 15 | 328 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O08342 | 6.07e-74 | 130 | 458 | 39 | 372 | Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1 |
P28623 | 1.23e-55 | 134 | 474 | 46 | 359 | Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2 |
P28621 | 9.54e-54 | 130 | 474 | 41 | 361 | Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1 |
A7LXT7 | 6.50e-47 | 3 | 457 | 22 | 477 | 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 |
P10477 | 3.33e-42 | 133 | 474 | 59 | 372 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000002 | 1.000059 | 0.000000 | 0.000000 | 0.000000 |
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