Species | Pseudomonas_E bubulae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E bubulae | |||||||||||
CAZyme ID | MGYG000000657_00320 | |||||||||||
CAZy Family | GH50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 8841; End: 11192 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH50 | 77 | 735 | 9.1e-269 | 0.9800918836140888 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17992 | Agarase_CBM | 2.46e-10 | 73 | 182 | 42 | 152 | Agarase CBM like domain. This is the N-terminal CBM-like domain in exo-beta-agarase proteins (EC:3.2.1.81) found in the marine microbe Saccharophagus degradans. This enzyme catalyzes a critical step in the metabolism of agarose by S. degradans through cleaving agarose oligomers into neoagarobiose products that can be further processed into monomers. The CBM-like domain is structurally very similar to some CBM families. A loop in the CBM-like domain is involved in forming the roof of the active site channel. The contribution of the CBM-like domain to formation of the active site of the enzyme supports a role in substrate recognition explaining the exo-mode of beta-agarase action. |
pfam02449 | Glyco_hydro_42 | 0.001 | 464 | 658 | 118 | 294 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QPL30772.1 | 0.0 | 1 | 783 | 1 | 783 |
SDU62850.1 | 0.0 | 1 | 783 | 1 | 783 |
ARQ73663.1 | 0.0 | 1 | 783 | 1 | 783 |
QPC34815.1 | 0.0 | 1 | 783 | 1 | 783 |
ASC88188.1 | 0.0 | 1 | 783 | 1 | 783 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4BQ2_A | 2.91e-115 | 83 | 733 | 62 | 739 | Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40] |
4BQ4_A | 8.02e-115 | 83 | 733 | 62 | 739 | Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ4_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40] |
5Z6P_A | 5.04e-105 | 73 | 733 | 78 | 755 | Thecrystal structure of an agarase, AgWH50C [Agarivorans gilvus],5Z6P_B The crystal structure of an agarase, AgWH50C [Agarivorans gilvus] |
6XJ9_A | 1.22e-98 | 83 | 733 | 81 | 755 | Structureof PfGH50B [Pseudoalteromonas fuliginea],6XJ9_B Structure of PfGH50B [Pseudoalteromonas fuliginea] |
5T3B_A | 2.18e-14 | 255 | 733 | 84 | 469 | ChainA, Glycoside Hydrolase [Phocaeicola plebeius],5T3B_B Chain B, Glycoside Hydrolase [Phocaeicola plebeius] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48840 | 2.53e-112 | 83 | 733 | 290 | 945 | Beta-agarase B OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaB PE=3 SV=1 |
P48839 | 6.28e-73 | 26 | 738 | 214 | 914 | Beta-agarase A OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000367 | 0.998876 | 0.000205 | 0.000198 | 0.000178 | 0.000154 |
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