Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; | |||||||||||
CAZyme ID | MGYG000002212_01943 | |||||||||||
CAZy Family | GH120 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2; End: 1063 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14251 | PL-6 | 0.001 | 25 | 75 | 8 | 59 | Polysaccharide Lyase Family 6. Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QJU15009.1 | 1.64e-189 | 1 | 353 | 1 | 346 |
QQQ92440.1 | 3.78e-188 | 1 | 353 | 1 | 346 |
ASU27696.1 | 3.78e-188 | 1 | 353 | 1 | 346 |
ANU74887.1 | 3.78e-188 | 1 | 353 | 1 | 346 |
QIB58251.1 | 3.78e-188 | 1 | 353 | 1 | 346 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VST_A | 8.95e-109 | 1 | 353 | 1 | 357 | Thecomplex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VST_B The complex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VST_C The complex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VST_D The complex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_A The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_B The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_C The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_D The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_A The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_B The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_C The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_D The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000018 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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