Species | Phocaeicola sp900066445 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900066445 | |||||||||||
CAZyme ID | MGYG000000042_02924 | |||||||||||
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: 4622; End: 6154 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 157 | 476 | 1e-88 | 0.9818840579710145 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00150 | Cellulase | 4.04e-44 | 151 | 421 | 10 | 240 | Cellulase (glycosyl hydrolase family 5). |
cd14948 | BACON | 1.38e-15 | 41 | 118 | 7 | 82 | 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. |
COG2730 | BglC | 8.64e-15 | 144 | 418 | 54 | 322 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
pfam19190 | BACON_2 | 1.16e-09 | 41 | 121 | 7 | 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 | 4.25e-09 | 60 | 110 | 1 | 51 | 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 |
---|---|---|---|---|---|
QGY45078.1 | 1.01e-116 | 1 | 510 | 1 | 492 |
QRM99680.1 | 5.40e-109 | 48 | 504 | 134 | 567 |
QEL01247.1 | 7.62e-109 | 129 | 510 | 51 | 409 |
QBJ18684.1 | 4.61e-102 | 50 | 510 | 147 | 575 |
QPH58994.1 | 4.61e-102 | 50 | 510 | 147 | 575 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5OYC_A | 1.01e-84 | 129 | 503 | 40 | 393 | 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 | 7.87e-84 | 129 | 503 | 40 | 393 | 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] |
4W8A_A | 3.68e-74 | 132 | 510 | 1 | 378 | 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] |
3ZMR_A | 4.41e-58 | 38 | 485 | 12 | 448 | Bacteroidesovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus],3ZMR_B Bacteroides ovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus] |
6WQY_A | 2.37e-53 | 135 | 479 | 25 | 349 | ChainA, Cellulase [Phocaeicola salanitronis DSM 18170] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A7LXT7 | 2.24e-57 | 3 | 485 | 17 | 483 | 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 |
O08342 | 2.84e-47 | 134 | 502 | 40 | 398 | Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1 |
P28621 | 7.76e-40 | 136 | 507 | 44 | 378 | Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1 |
P54937 | 1.03e-39 | 132 | 418 | 37 | 311 | Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1 |
P10477 | 5.94e-39 | 134 | 503 | 57 | 385 | 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 | 0.000003 | 1.000048 | 0.000000 | 0.000000 | 0.000000 |
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