| Species | Dysgonomonas gadei | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas gadei | |||||||||||
| CAZyme ID | MGYG000001376_01586 | |||||||||||
| CAZy Family | GH146 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 292427; End: 294754 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH146 | 42 | 552 | 6.5e-198 | 0.9980119284294234 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam07944 | Glyco_hydro_127 | 0.0 | 42 | 552 | 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 | 3.19e-132 | 35 | 557 | 9 | 506 | Uncharacterized conserved protein, DUF1680 family [Function unknown]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUT89366.1 | 3.64e-237 | 36 | 775 | 34 | 776 |
| ALJ59598.1 | 7.30e-237 | 36 | 775 | 34 | 776 |
| QIX60435.1 | 5.33e-235 | 38 | 765 | 50 | 781 |
| AYB34620.1 | 1.92e-232 | 37 | 774 | 58 | 798 |
| QEH43070.1 | 2.29e-230 | 3 | 774 | 2 | 787 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6YQH_AAA | 4.90e-167 | 31 | 696 | 21 | 728 | ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482] |
| 5OPJ_A | 1.47e-162 | 31 | 696 | 21 | 728 | Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron] |
| 5MQO_A | 4.13e-16 | 178 | 550 | 196 | 605 | Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron] |
| 3WRE_A | 2.96e-13 | 174 | 603 | 144 | 642 | 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] |
| 3WKW_A | 3.00e-13 | 174 | 603 | 144 | 642 | Crystalstructure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum ligand free form [Bifidobacterium longum subsp. longum JCM 1217],3WKX_A Crystal structure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum arabinose complex form [Bifidobacterium longum subsp. longum JCM 1217],7BZL_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7DIF_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXV_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXW_A Chain A, 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 | 1.62e-12 | 174 | 603 | 144 | 642 | 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 |
|---|---|---|---|---|---|
| 0.489871 | 0.497312 | 0.011370 | 0.000454 | 0.000367 | 0.000619 |
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