Species | Massilioclostridium coli | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilioclostridium; Massilioclostridium coli | |||||||||||
CAZyme ID | MGYG000001560_01716 | |||||||||||
CAZy Family | GH78 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 298267; End: 301563 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH78 | 1 | 371 | 7.4e-59 | 0.7619047619047619 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17389 | Bac_rhamnosid6H | 6.05e-08 | 1 | 307 | 12 | 336 | Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria. |
pfam17390 | Bac_rhamnosid_C | 1.20e-06 | 313 | 380 | 1 | 70 | Bacterial alpha-L-rhamnosidase C-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria. |
pfam17996 | CE2_N | 0.003 | 645 | 718 | 15 | 81 | Carbohydrate esterase 2 N-terminal. This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyses the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEC76313.1 | 1.00e-225 | 1 | 614 | 221 | 847 |
QGA24541.1 | 2.42e-205 | 2 | 604 | 213 | 819 |
QMW04815.1 | 1.27e-182 | 1 | 604 | 212 | 815 |
ATP56756.1 | 1.83e-181 | 2 | 604 | 210 | 817 |
ACT93515.1 | 3.06e-169 | 1 | 604 | 229 | 830 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3CIH_A | 2.44e-21 | 2 | 356 | 311 | 680 | Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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