| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000298815 |
| Family | GH13 |
| Protein Properties | Length: 1023 Molecular Weight: 114304 Isoelectric Point: 6.1505 |
| Chromosome | Chromosome/Scaffold: 011694390 Start: 6567 End: 16942 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH13 | 637 | 941 | 7.3e-39 |
| KGGWYNILKQSVQDLASSGITHVWLPPSSHAASDEGYMPGRLYDLNSKFGNKDELKSLVSAYRNSGIQSVADIVINHRTAEKQDERGIWCIFEGGTDDDR LDWGPSLICGDDTKYSDGKGNPDTGEDFGGAPDIDHKNTRVQKELSDWMNWLKTEIGFSGWRFDFVKGYAPEYTKLYMTNTSPNFAVGELWNSLSYGSDG KPNPDQDAHRQALVGWVESAGGGVTAFDFTTKGILQAAVQGELWRLKDSNGGAPGMIGLKPGSSVTFIDNHDTGSTQHLWPFPSDKVMQGYAYILTHPGI PSIFY | |||
| GH13 | 275 | 582 | 5.9e-39 |
| EGGWYKSLSQSIPQQLASSGITHVWLPPPSHSVSPQGYMPGRLYDLNASRYGNQDELKALINTFHDNGIQSIADIVINHRCAEKKDERGIWCIFEGGTPD DRLDWGPSLICSDDTAYSNGKGNPDTGADFSAAPDIDHINTRVQRELSDWMNWLKTEIGFNGWRFDFVKGYAPEFTKLFVTNTRPSFSVGELWNSLAYGS DGKLEYNQDAHRRALVGWVEGAGGDVTAFDFTTKGILQAAVQGELWRMKDSNGGAPGMIGLSPGKSVTFVDNHDTGSTQNMWPFPSDKVMQGYAYILTHP GIPSIFYD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1023 Download |
| MDSFWSHNAA PGSWDFLVAV YFAFGFFAAR LIFDRFIFRN ISVWLLRKGS ASLKLDMATR 60 AKIVKCSESM WKLTYYATVE ACILSITYHE PWFTDTKEYF KGWPNQELRL VIHTVGLNSP 120 KLLASHKAFL YVSVWILQLQ HCCPPYMGDS KEGFLSDDVS PCNYCSPDWV LIHNKVYFSF 180 FRIGSIILAL HDGSDVFMEA AKVFKYSEKE LAASVFFGFF AVSWAILRLI FFPFWVISAS 240 RSALMIQRTM IRRNISPSSF CVAVLGFNWE SWKEEGGWYK SLSQSIPQQL ASSGITHVWL 300 PPPSHSVSPQ GYMPGRLYDL NASRYGNQDE LKALINTFHD NGIQSIADIV INHRCAEKKD 360 ERGIWCIFEG GTPDDRLDWG PSLICSDDTA YSNGKGNPDT GADFSAAPDI DHINTRVQRE 420 LSDWMNWLKT EIGFNGWRFD FVKGYAPEFT KLFVTNTRPS FSVGELWNSL AYGSDGKLEY 480 NQDAHRRALV GWVEGAGGDV TAFDFTTKGI LQAAVQGELW RMKDSNGGAP GMIGLSPGKS 540 VTFVDNHDTG STQNMWPFPS DKVMQGYAYI LTHPGIPSIF YDHYFDWGLK EEITKLVAIR 600 LRNGVGPDSA LRILASDADL YVAATDEKII AKIGPRKGGW YNILKQSVQD LASSGITHVW 660 LPPSSHAASD EGYMPGRLYD LNSKFGNKDE LKSLVSAYRN SGIQSVADIV INHRTAEKQD 720 ERGIWCIFEG GTDDDRLDWG PSLICGDDTK YSDGKGNPDT GEDFGGAPDI DHKNTRVQKE 780 LSDWMNWLKT EIGFSGWRFD FVKGYAPEYT KLYMTNTSPN FAVGELWNSL SYGSDGKPNP 840 DQDAHRQALV GWVESAGGGV TAFDFTTKGI LQAAVQGELW RLKDSNGGAP GMIGLKPGSS 900 VTFIDNHDTG STQHLWPFPS DKVMQGYAYI LTHPGIPSIF YDHFFDWGLK GEISKLTAIR 960 SRNGIKPDSA LRILAADADV YVASIDEKII VKIGPKMDLG QLIPPNFQVS TSGKDYAVWE 1020 RKA |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02361 | PLN02361 | 6.0e-130 | 637 | 1021 | 390 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-143 | 635 | 971 | 340 | + 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. | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-149 | 266 | 611 | 349 | + 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 | 0 | 266 | 636 | 374 | + alpha-amylase; Provisional | ||
| PLN00196 | PLN00196 | 0 | 638 | 1021 | 388 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005975 | carbohydrate metabolic process |
| GO:0016021 | integral to membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAX33232.1 | 0 | 266 | 636 | 8 | 367 | secreted alpha-amylase [Malus x domestica] |
| GenBank | AAX33232.1 | 0 | 636 | 1023 | 16 | 394 | secreted alpha-amylase [Malus x domestica] |
| EMBL | CAN77038.1 | 0 | 220 | 660 | 1 | 439 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN77038.1 | 0 | 636 | 1022 | 55 | 442 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002285213.1 | 0 | 636 | 1022 | 37 | 424 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 636 | 1021 | 14 | 402 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
| PDB | 1bg9_A | 0 | 262 | 636 | 2 | 377 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
| PDB | 1ava_B | 0 | 636 | 1021 | 14 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_B | 0 | 262 | 636 | 2 | 377 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 636 | 1021 | 14 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
