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CAZyme Information: MGYG000003208_02372
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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 | Pseudomonas_E extremaustralis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis | |||||||||||
| CAZyme ID | MGYG000003208_02372 | |||||||||||
| CAZy Family | GH50 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 253277; End: 255574 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH50 | 75 | 716 | 1.9e-271 | 0.9800918836140888 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam02449 | Glyco_hydro_42 | 3.23e-05 | 374 | 574 | 48 | 231 | 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. |
| pfam17992 | Agarase_CBM | 6.53e-05 | 37 | 149 | 11 | 121 | 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. |
| cd19608 | GH113_mannanase-like | 0.007 | 615 | 688 | 215 | 292 | Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SDF49772.1 | 0.0 | 1 | 765 | 1 | 765 |
| QTV18625.1 | 0.0 | 1 | 765 | 1 | 765 |
| AYF47303.1 | 0.0 | 1 | 765 | 1 | 765 |
| QJI15940.1 | 0.0 | 1 | 765 | 1 | 765 |
| AZF62363.1 | 0.0 | 1 | 765 | 1 | 765 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4BQ2_A | 5.06e-109 | 82 | 715 | 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 | 1.39e-108 | 82 | 715 | 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] |
| 6XJ9_A | 2.10e-99 | 72 | 725 | 72 | 765 | Structureof PfGH50B [Pseudoalteromonas fuliginea],6XJ9_B Structure of PfGH50B [Pseudoalteromonas fuliginea] |
| 5Z6P_A | 8.22e-98 | 72 | 715 | 78 | 755 | Thecrystal structure of an agarase, AgWH50C [Agarivorans gilvus],5Z6P_B The crystal structure of an agarase, AgWH50C [Agarivorans gilvus] |
| 5T3B_A | 1.42e-12 | 254 | 679 | 82 | 442 | ChainA, Glycoside Hydrolase [Phocaeicola plebeius],5T3B_B Chain B, Glycoside Hydrolase [Phocaeicola plebeius] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P48840 | 6.68e-108 | 82 | 715 | 290 | 945 | Beta-agarase B OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaB PE=3 SV=1 |
| P48839 | 4.93e-74 | 25 | 715 | 214 | 909 | Beta-agarase A OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaA PE=3 SV=1 |
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 |
|---|---|---|---|---|---|
| 0.000295 | 0.999006 | 0.000182 | 0.000170 | 0.000164 | 0.000152 |