Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; | |||||||||||
CAZyme ID | MGYG000000720_01138 | |||||||||||
CAZy Family | GH51 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 49128; End: 50675 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH51 | 118 | 512 | 1.5e-32 | 0.6031746031746031 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3534 | AbfA | 2.78e-13 | 118 | 515 | 78 | 501 | Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism]. |
smart00813 | Alpha-L-AF_C | 6.70e-05 | 322 | 506 | 1 | 189 | Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides. |
cd21510 | agarase_cat | 0.005 | 211 | 403 | 102 | 319 | alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVM44875.1 | 4.83e-125 | 20 | 510 | 205 | 701 |
SDT99044.1 | 5.21e-84 | 3 | 515 | 10 | 540 |
QDU72262.1 | 1.59e-71 | 11 | 490 | 13 | 516 |
QDU70476.1 | 2.40e-67 | 29 | 510 | 41 | 540 |
AHF91282.1 | 3.74e-26 | 119 | 404 | 122 | 418 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Y2W_A | 8.71e-09 | 118 | 347 | 120 | 363 | Elucidationof the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_B Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_C Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_D Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_E Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_F Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q841V6 | 4.72e-08 | 118 | 347 | 120 | 363 | Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Bifidobacterium longum OX=216816 GN=abfB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000692 | 0.998356 | 0.000229 | 0.000279 | 0.000234 | 0.000199 |
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