Species | Phytophthora palmivora | |||||||||||
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Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora palmivora | |||||||||||
CAZyme ID | PHPALM_12412-t46_1-p1 | |||||||||||
CAZy Family | AA17 | |||||||||||
CAZyme Description | Alpha-glucosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.1:4 | 3.2.1.98:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM25 | 145 | 219 | 7.3e-17 | 0.9230769230769231 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
200456 | AmyAc_bac_euk_AmyA | 3.60e-23 | 246 | 305 | 1 | 53 | Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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. |
198134 | CBM_25 | 2.65e-10 | 43 | 116 | 15 | 82 | Carbohydrate binding domain. |
407028 | CBM53 | 2.89e-10 | 38 | 114 | 1 | 75 | Starch/carbohydrate-binding module (family 53). |
198134 | CBM_25 | 3.91e-10 | 149 | 218 | 14 | 78 | Carbohydrate binding domain. |
367491 | CBM_25 | 2.48e-09 | 141 | 218 | 3 | 76 | Carbohydrate binding domain (family 25). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
9.18e-30 | 25 | 223 | 48 | 241 | |
1.72e-29 | 20 | 223 | 591 | 794 | |
1.78e-23 | 21 | 238 | 634 | 881 | |
1.09e-22 | 21 | 238 | 634 | 881 | |
4.04e-22 | 33 | 237 | 986 | 1185 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.00e-11 | 137 | 222 | 5 | 86 | Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3X_A Chain A, Alpha-amylase G-6 [Halalkalibacterium halodurans C-125],2C3X_B Chain B, Alpha-amylase G-6 [Halalkalibacterium halodurans C-125] |
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8.25e-11 | 137 | 222 | 5 | 86 | Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125] |
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5.94e-09 | 248 | 305 | 12 | 64 | Recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris [Oryzias latipes] |
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5.78e-08 | 246 | 305 | 10 | 62 | YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor] |
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5.78e-08 | 246 | 305 | 10 | 62 | TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.19e-16 | 21 | 218 | 889 | 1167 | Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1 |
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3.96e-09 | 218 | 305 | 2 | 82 | Alpha-amylase-related protein OS=Drosophila subobscura OX=7241 GN=Amyrel PE=3 SV=1 |
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9.47e-09 | 218 | 305 | 2 | 82 | Alpha-amylase-related protein OS=Drosophila varians OX=30050 GN=Amyrel PE=3 SV=1 |
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1.26e-08 | 244 | 305 | 27 | 81 | Alpha-amylase-related protein OS=Drosophila melanogaster OX=7227 GN=Amyrel PE=2 SV=2 |
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1.27e-08 | 244 | 305 | 9 | 63 | Alpha-amylase (Fragment) OS=Dermatophagoides pteronyssinus OX=6956 PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
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0.000241 | 0.999743 | CS pos: 25-26. Pr: 0.9693 |
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