Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr1g019440.1 |
Family | GH13 |
Protein Properties | Length: 422 Molecular Weight: 46714.6 Isoelectric Point: 4.9879 |
Chromosome | Chromosome/Scaffold: 1 Start: 6026886 End: 6029202 |
Description | alpha-amylase-like |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 37 | 342 | 9.99995e-41 |
KGGWYNSLKNLIPDLANAGITHVWLPPPSQSVGPQGYLPGRLYDLDASKYGSKDDLKSLIAAFKDKGINCLADIVINHRTAERKDDRGIYCLFEGGTPDS KLDWGPSFICKDDTAYSDGTGNLDSGEGYQAAPDIDHLNPQVQKELSEWMNWLKTEIGFSGWRFDFVKGYAPSITKIYMENTSPDFAVGEYWNSLSYGQD GKLNYNQDAARGELVNWVENGGGVVNAFDFTTKGILQAAVQGELWRLKDSNGKPPGLIGIKPENGATFIDNHDTGSTQKLWPFPSDKVMQGYAYILTHPG TPSIFY |
Full Sequence |
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Protein Sequence Length: 422 Download |
MNSLPWLSLF CFCLSIFPLL ASSTLLFQGF NWESSNKGGW YNSLKNLIPD LANAGITHVW 60 LPPPSQSVGP QGYLPGRLYD LDASKYGSKD DLKSLIAAFK DKGINCLADI VINHRTAERK 120 DDRGIYCLFE GGTPDSKLDW GPSFICKDDT AYSDGTGNLD SGEGYQAAPD IDHLNPQVQK 180 ELSEWMNWLK TEIGFSGWRF DFVKGYAPSI TKIYMENTSP DFAVGEYWNS LSYGQDGKLN 240 YNQDAARGEL VNWVENGGGV VNAFDFTTKG ILQAAVQGEL WRLKDSNGKP PGLIGIKPEN 300 GATFIDNHDT GSTQKLWPFP SDKVMQGYAY ILTHPGTPSI FYDHFFDWGL KDQIAKLTAI 360 RQRNGINMKS TVNILAADAD LYVAKIDNKI IVKIGPRMDL GNLIPSNFHV ATSGQDYAVW 420 E* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-49 | 26 | 363 | 408 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 1.0e-141 | 25 | 421 | 398 | + alpha-amylase | ||
PLN02361 | PLN02361 | 1.0e-145 | 25 | 421 | 402 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 7.0e-152 | 26 | 372 | 350 | + 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 | 7 | 421 | 419 | + alpha-amylase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004556 | alpha-amylase activity |
GO:0005509 | calcium ion binding |
GO:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PRF/SEQDB | 0 | 1 | 421 | 1 | 421 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
DDBJ | BAA33879.1 | 0 | 1 | 421 | 1 | 420 | alpha-amylase [Phaseolus vulgaris] |
DDBJ | BAC76729.1 | 0 | 1 | 421 | 1 | 421 | alpha-amylase [Vigna angularis] |
Swiss-Prot | P17859 | 0 | 1 | 421 | 1 | 421 | AMYA_VIGMU RecName: Full=Alpha-amylase; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; Flags: Precursor |
RefSeq | XP_002327139.1 | 0 | 7 | 420 | 1 | 421 | predicted protein [Populus trichocarpa] |
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 | 25 | 421 | 2 | 401 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1ava_B | 0 | 25 | 421 | 2 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 25 | 421 | 2 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 25 | 421 | 2 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 25 | 421 | 3 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |