Species | Streptococcus thermophilus | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus thermophilus | |||||||||||
CAZyme ID | MGYG000004345_01780 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Pullulanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5345; End: 5710 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 1 | 117 | 1.1e-44 | 0.3767605633802817 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR02102 | pullulan_Gpos | 1.88e-75 | 1 | 121 | 618 | 738 | pullulanase, extracellular, Gram-positive. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (. |
cd11341 | AmyAc_Pullulanase_LD-like | 2.56e-36 | 1 | 121 | 173 | 292 | Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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. |
COG1523 | PulA | 1.35e-29 | 1 | 121 | 335 | 446 | Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism]. |
TIGR02104 | pulA_typeI | 7.74e-21 | 1 | 115 | 295 | 407 | pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. |
PLN02877 | PLN02877 | 1.06e-06 | 1 | 107 | 535 | 650 | alpha-amylase/limit dextrinase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AQW32990.1 | 6.54e-86 | 1 | 121 | 1 | 121 |
CCC19921.1 | 6.54e-86 | 1 | 121 | 1 | 121 |
QKM74521.1 | 6.54e-86 | 1 | 121 | 1 | 121 |
AIC25142.1 | 6.54e-86 | 1 | 121 | 1 | 121 |
ALD16896.1 | 6.54e-86 | 1 | 121 | 1 | 121 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2YA2_A | 1.67e-60 | 1 | 121 | 319 | 439 | CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4] |
2YA0_A | 1.80e-60 | 1 | 121 | 318 | 438 | CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4] |
2YA1_A | 1.48e-59 | 1 | 121 | 625 | 745 | Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4] |
3FAW_A | 2.62e-57 | 1 | 121 | 433 | 553 | CrystalStructure of the Group B Streptococcus Pullulanase SAP [Streptococcus agalactiae COH1],3FAX_A The crystal structure of GBS pullulanase SAP in complex with maltotetraose [Streptococcus agalactiae COH1] |
7LSA_A | 8.80e-16 | 1 | 121 | 368 | 495 | ChainA, Pullulanase [Ruminococcus bromii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A0A0H2ZL64 | 7.67e-59 | 1 | 121 | 739 | 859 | Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1 |
Q9F930 | 7.70e-59 | 1 | 121 | 761 | 881 | Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1 |
A0A0H2UNG0 | 1.05e-58 | 1 | 121 | 754 | 874 | Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1 |
P07811 | 3.81e-13 | 1 | 97 | 670 | 762 | Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1 |
P07206 | 5.20e-13 | 1 | 97 | 660 | 752 | Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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