Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; | |||||||||||
CAZyme ID | MGYG000004880_00533 | |||||||||||
CAZy Family | GH5 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 68122; End: 69648 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 160 | 467 | 1.1e-93 | 0.9855072463768116 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00150 | Cellulase | 2.28e-51 | 150 | 467 | 1 | 269 | Cellulase (glycosyl hydrolase family 5). |
COG2730 | BglC | 3.15e-24 | 135 | 494 | 46 | 386 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
cd14948 | BACON | 6.87e-13 | 37 | 118 | 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. |
pfam19190 | BACON_2 | 3.45e-07 | 38 | 120 | 2 | 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. |
pfam13004 | BACON | 5.83e-04 | 67 | 118 | 7 | 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 |
---|---|---|---|---|---|
ADB44000.1 | 8.76e-162 | 63 | 507 | 69 | 515 |
VEH16026.1 | 7.33e-131 | 69 | 503 | 186 | 604 |
QDM10331.1 | 6.13e-96 | 18 | 507 | 22 | 492 |
QNL39874.1 | 1.22e-95 | 65 | 507 | 66 | 492 |
QGY45078.1 | 2.47e-91 | 38 | 507 | 36 | 491 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4W8A_A | 6.92e-163 | 131 | 507 | 1 | 377 | Crystalstructure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in the native form [uncultured bacterium],4W8B_A Crystal structure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in complex with XXLG [uncultured bacterium] |
5OYC_A | 9.16e-74 | 124 | 503 | 36 | 395 | GH5endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYC_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107] |
6HA9_A | 7.07e-73 | 124 | 503 | 36 | 395 | Structureof an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HA9_B Structure of an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_A Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_B Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107] |
2JEP_A | 5.08e-68 | 133 | 500 | 35 | 393 | 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] |
6Q1I_A | 3.59e-57 | 129 | 502 | 10 | 354 | GH5-4broad specificity endoglucanase from Clostrdium longisporum [Clostridium longisporum],6Q1I_B GH5-4 broad specificity endoglucanase from Clostrdium longisporum [Clostridium longisporum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O08342 | 4.65e-61 | 133 | 500 | 40 | 398 | Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1 |
P54937 | 8.03e-56 | 98 | 502 | 7 | 379 | Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1 |
P17901 | 3.57e-50 | 143 | 474 | 57 | 375 | Endoglucanase A OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCA PE=1 SV=1 |
P23660 | 1.16e-48 | 133 | 502 | 27 | 364 | Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1 |
A7LXT7 | 1.13e-47 | 12 | 471 | 23 | 479 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000000 | 1.000019 | 0.000000 | 0.000000 | 0.000000 |
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