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CAZyme Information: MGYG000003693_02537
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Phocaeicola plebeius_A | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola plebeius_A | |||||||||||
| CAZyme ID | MGYG000003693_02537 | |||||||||||
| CAZy Family | GH51 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 27266; End: 29776 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH51 | 385 | 829 | 8.5e-103 | 0.680952380952381 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3534 | AbfA | 2.02e-37 | 388 | 832 | 33 | 501 | Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism]. |
| pfam06964 | Alpha-L-AF_C | 9.23e-37 | 648 | 823 | 1 | 192 | Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides. |
| smart00813 | Alpha-L-AF_C | 7.98e-30 | 648 | 823 | 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. |
| pfam02018 | CBM_4_9 | 1.71e-06 | 238 | 379 | 1 | 129 | Carbohydrate binding domain. This family includes diverse carbohydrate binding domains. |
| cd18622 | GH32_Inu-like | 2.05e-06 | 88 | 123 | 10 | 49 | glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AFK82647.1 | 0.0 | 1 | 836 | 1 | 836 |
| ADY34735.1 | 0.0 | 1 | 833 | 1 | 829 |
| QJR78261.1 | 0.0 | 9 | 833 | 9 | 831 |
| QJR69776.1 | 0.0 | 9 | 833 | 9 | 831 |
| AII66682.1 | 0.0 | 9 | 833 | 9 | 831 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6ZPS_AAA | 2.74e-87 | 206 | 832 | 3 | 627 | ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus] |
| 2VRQ_A | 1.81e-13 | 404 | 563 | 50 | 177 | StructureOf An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_B Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_C Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus] |
| 6ZT6_A | 3.17e-13 | 404 | 563 | 50 | 177 | ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus] |
| 6ZT8_A | 3.17e-13 | 404 | 563 | 50 | 177 | ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus] |
| 6ZTA_A | 3.17e-13 | 404 | 563 | 50 | 177 | ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P82593 | 9.10e-138 | 197 | 733 | 19 | 547 | Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1 |
| Q9SG80 | 5.01e-85 | 202 | 736 | 41 | 553 | Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1 |
| Q8VZR2 | 1.21e-80 | 200 | 736 | 38 | 552 | Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1 |
| Q0CTV2 | 1.03e-73 | 204 | 729 | 26 | 530 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=abfA PE=3 SV=1 |
| B8NKA3 | 1.05e-73 | 204 | 729 | 26 | 531 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abfA PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000334 | 0.998726 | 0.000372 | 0.000211 | 0.000175 | 0.000158 |