Species | UMGS856 sp900546265 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS856; UMGS856 sp900546265 | |||||||||||
CAZyme ID | MGYG000002711_02403 | |||||||||||
CAZy Family | GH129 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 41096; End: 42985 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH129 | 90 | 624 | 3.1e-104 | 0.8592233009708737 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14244 | GH_101_like | 2.54e-20 | 325 | 464 | 40 | 189 | Endo-a-N-acetylgalactosaminidase and related glcyosyl hydrolases. This family contains the enzymatically active domain of cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins (EC:3.2.1.97). It has been classified as glycosyl hydrolase family 101 in the Cazy resource. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae and other commensal human bacteria is largely determined by their ability to degrade host glycoproteins and to metabolize the resultant carbohydrates. |
cd11336 | AmyAc_MTSase | 0.003 | 333 | 366 | 46 | 77 | Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase). Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
PRK14511 | PRK14511 | 0.003 | 333 | 366 | 52 | 83 | malto-oligosyltrehalose synthase. |
pfam12905 | Glyco_hydro_101 | 0.007 | 324 | 387 | 61 | 125 | Endo-alpha-N-acetylgalactosaminidase. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae is largely determined by the ability to degrade host glycoproteins and to metabolize the resultant carbohydrates. This family is the enzymatic region, EC:3.2.1.97, of the cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins. This reaction is exemplified by the S. pneumoniae protein Endo-alpha-N-acetylgalactosaminidase, where Asp764 is the catalytic nucleophile-base and Glu796 the catalytic proton donor. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUH27706.1 | 4.28e-148 | 41 | 624 | 41 | 621 |
QUH27660.1 | 1.41e-147 | 24 | 624 | 14 | 626 |
QNK55038.1 | 3.66e-125 | 75 | 624 | 77 | 624 |
QTH41330.1 | 2.63e-124 | 24 | 624 | 28 | 624 |
QJD87097.1 | 3.90e-120 | 54 | 624 | 58 | 625 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5WZN_A | 1.54e-114 | 56 | 624 | 46 | 628 | Alpha-N-acetylgalactosaminidaseNagBb from Bifidobacterium bifidum - GalNAc complex [Bifidobacterium bifidum],5WZN_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - GalNAc complex [Bifidobacterium bifidum],5WZP_A Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - ligand free [Bifidobacterium bifidum],5WZP_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - ligand free [Bifidobacterium bifidum],5WZR_A Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - Gal-NHAc-DNJ complex [Bifidobacterium bifidum],5WZR_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - Gal-NHAc-DNJ complex [Bifidobacterium bifidum] |
5WZQ_A | 6.57e-109 | 56 | 624 | 46 | 628 | Alpha-N-acetylgalactosaminidaseNagBb from Bifidobacterium bifidum - quadruple mutant [Bifidobacterium bifidum],5WZQ_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - quadruple mutant [Bifidobacterium bifidum] |
5OPQ_A | 6.27e-16 | 49 | 629 | 84 | 666 | A3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans],5OPQ_B A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans],5OPQ_C A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans],5OPQ_D A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000055 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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