Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_336273g0010 |
Family | GH13 |
Protein Properties | Length: 241 Molecular Weight: 25971 Isoelectric Point: 4.5887 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 70 | 232 | 5.6e-26 |
LKGIVEDAAEAGITDVWFPPPSQSVAPQGYMPGKLYDLDSSKYGNEQQLKEVVAAFHQKGIGCVGDIVINHRCGTKKDDKGMWCVFEGGKGDGSLDWGPW AVTINDQPFACGSGQADTGGDYTAAPDIDHTNPKIQQDLSDWMNWLKSNVGFDGWRFDFAKGY |
Full Sequence |
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Protein Sequence Length: 241 Download |
MAKFKLVFVF LLSSIIINAE AQAQAPTPTS GASRGSAGNN ISANTDALNT VLLQGFNWES 60 SKSSSWYNVL KGIVEDAAEA GITDVWFPPP SQSVAPQGYM PGKLYDLDSS KYGNEQQLKE 120 VVAAFHQKGI GCVGDIVINH RCGTKKDDKG MWCVFEGGKG DGSLDWGPWA VTINDQPFAC 180 GSGQADTGGD YTAAPDIDHT NPKIQQDLSD WMNWLKSNVG FDGWRFDFAK GYAGNLLGVY 240 L |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11318 | AmyAc_bac_fung_AmyA | 4.0e-18 | 49 | 143 | 106 | + Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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. | ||
PLN02361 | PLN02361 | 2.0e-50 | 51 | 241 | 193 | + alpha-amylase | ||
PLN02784 | PLN02784 | 3.0e-55 | 51 | 241 | 191 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-73 | 51 | 240 | 192 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 from bacteria, archaea, water fleas, and plants. 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. | ||
PLN00196 | PLN00196 | 2.0e-86 | 43 | 241 | 200 | + alpha-amylase; Provisional |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABK24287.1 | 0 | 1 | 240 | 1 | 234 | unknown [Picea sitchensis] |
GenBank | ABK24434.1 | 0 | 1 | 241 | 1 | 234 | unknown [Picea sitchensis] |
GenBank | ABR16554.1 | 0 | 1 | 240 | 1 | 234 | unknown [Picea sitchensis] |
RefSeq | XP_001754460.1 | 0 | 55 | 241 | 1 | 187 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002510218.1 | 0 | 51 | 241 | 21 | 212 | alpha-amylase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1bg9_A | 0 | 51 | 241 | 2 | 193 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
PDB | 1ava_B | 0 | 51 | 241 | 2 | 193 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 51 | 241 | 2 | 193 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 51 | 241 | 2 | 193 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 49 | 241 | 1 | 194 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |