Species | Bacteroides acidifaciens | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides acidifaciens | |||||||||||
CAZyme ID | MGYG000000054_04403 | |||||||||||
CAZy Family | GH127 | |||||||||||
CAZyme Description | Non-reducing end beta-L-arabinofuranosidase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 586; End: 2682 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH127 | 44 | 607 | 7.7e-193 | 0.9980916030534351 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07944 | Glyco_hydro_127 | 0.0 | 43 | 607 | 1 | 503 | Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context. |
COG3533 | COG3533 | 1.88e-135 | 49 | 694 | 21 | 585 | Uncharacterized conserved protein, DUF1680 family [Function unknown]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QIU95849.1 | 0.0 | 1 | 698 | 1 | 698 |
QUT23610.1 | 0.0 | 1 | 698 | 1 | 698 |
QDH55672.1 | 0.0 | 1 | 698 | 1 | 698 |
QUT29106.1 | 0.0 | 1 | 698 | 1 | 698 |
QUR43102.1 | 0.0 | 1 | 698 | 1 | 698 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MQO_A | 0.0 | 1 | 698 | 1 | 698 | Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron] |
4QJY_A | 1.68e-130 | 44 | 694 | 16 | 645 | Crystalstructure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus] |
4QK0_A | 2.44e-126 | 44 | 694 | 16 | 645 | Crystalstructure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_B Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_C Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_D Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus] |
6EX6_A | 1.14e-111 | 43 | 696 | 14 | 625 | TheGH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482],6EX6_B The GH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482] |
7EXU_A | 5.91e-84 | 76 | 692 | 51 | 654 | ChainA, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
E8MGH8 | 6.85e-83 | 76 | 692 | 51 | 654 | Non-reducing end beta-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000463 | 0.998637 | 0.000240 | 0.000231 | 0.000210 | 0.000194 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.