Species | Bacteroides finegoldii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides finegoldii | |||||||||||
CAZyme ID | MGYG000000029_02132 | |||||||||||
CAZy Family | GH78 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 86973; End: 89177 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH78 | 191 | 685 | 4.2e-116 | 0.9642857142857143 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17389 | Bac_rhamnosid6H | 4.49e-22 | 305 | 638 | 4 | 339 | 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 | 3.73e-06 | 641 | 677 | 1 | 38 | 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. |
COG4354 | COG4354 | 0.002 | 394 | 479 | 449 | 531 | Uncharacterized protein, contains GBA2_N and DUF608 domains [Function unknown]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNL37671.1 | 0.0 | 1 | 734 | 1 | 734 |
CBK65632.1 | 0.0 | 1 | 734 | 1 | 734 |
QRQ56933.1 | 0.0 | 1 | 734 | 1 | 734 |
SCV09640.1 | 0.0 | 1 | 734 | 1 | 734 |
ALJ45306.1 | 0.0 | 1 | 734 | 1 | 734 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3CIH_A | 0.0 | 6 | 734 | 3 | 731 | Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
2OKX_A | 5.12e-46 | 191 | 720 | 433 | 952 | Crystalstructure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1],2OKX_B Crystal structure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1] |
4XHC_A | 8.72e-28 | 310 | 638 | 212 | 541 | ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
T2KM26 | 3.35e-14 | 188 | 676 | 598 | 1109 | Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2 |
P9WF03 | 2.56e-10 | 139 | 677 | 322 | 853 | Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1 |
T2KPL4 | 2.42e-07 | 20 | 445 | 200 | 651 | Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000724 | 0.998263 | 0.000257 | 0.000260 | 0.000246 | 0.000231 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.