Species | Parabacteroides sp900547435 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900547435 | |||||||||||
CAZyme ID | MGYG000003091_00596 | |||||||||||
CAZy Family | GH127 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 26174; End: 27622 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH127 | 2 | 249 | 2.7e-86 | 0.4389312977099237 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3533 | COG3533 | 1.48e-75 | 2 | 323 | 284 | 585 | Uncharacterized conserved protein, DUF1680 family [Function unknown]. |
pfam07944 | Glyco_hydro_127 | 6.83e-75 | 2 | 249 | 282 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
SCD19473.1 | 6.75e-192 | 2 | 482 | 341 | 824 |
AIA99612.1 | 6.44e-174 | 2 | 476 | 351 | 824 |
QJE94520.1 | 6.76e-169 | 2 | 479 | 341 | 819 |
BBO34810.1 | 2.29e-165 | 2 | 478 | 341 | 824 |
QDV74096.1 | 1.48e-163 | 2 | 478 | 353 | 835 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6EX6_A | 4.15e-88 | 2 | 323 | 307 | 623 | TheGH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482],6EX6_B The GH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482] |
4QJY_A | 4.22e-66 | 2 | 325 | 325 | 647 | 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 | 2.27e-63 | 2 | 325 | 325 | 647 | 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] |
5MQO_A | 9.54e-52 | 2 | 323 | 373 | 694 | Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron] |
3WRE_A | 1.29e-44 | 2 | 314 | 330 | 647 | Thecrystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 [Bifidobacterium longum subsp. longum JCM 1217],3WRG_A The complex structure of HypBA1 with L-arabinose [Bifidobacterium longum subsp. longum JCM 1217] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
E8MGH8 | 7.08e-44 | 2 | 314 | 330 | 647 | 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 |
---|---|---|---|---|---|
1.000042 | 0.000003 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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