Basic Information | |
---|---|
Species | Medicago truncatula |
Cazyme ID | Medtr1g019480.1 |
Family | GH13 |
Protein Properties | Length: 403 Molecular Weight: 44871.8 Isoelectric Point: 5.4264 |
Chromosome | Chromosome/Scaffold: 1 Start: 6040975 End: 6042963 |
Description | alpha-amylase-like |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 46 | 323 | 9.5e-29 |
KTKVPDIADAGVEYVWLPPPSNSHDDGPQGYLPKRLYDLDTSKYGNKQELKSLVAAFREQGVKSISDIVINHRTAERLDNNGLSIFEGGTPDNRLDWDVS YICGNDVQFKGTGNNDTGDDWGGAPDVDHTNPKVQQELSDWMNWFTKNYVEKTSPDFTVGELYRNVELGSDGKPLANQDKHRETLVKWVNDAGGVVTTFD FTTKMILGAAVQGELWRMKDANGKPPGMIGIMPSNAVTFVDNHDTGSQKLWPFPDDKVMLGYVYILTHPGHPTIFYDH |
Full Sequence |
---|
Protein Sequence Length: 403 Download |
MKFLHSICFL CLCISIFPSF SSSAILFQGF KWASSEKEGG WWNFLKTKVP DIADAGVEYV 60 WLPPPSNSHD DGPQGYLPKR LYDLDTSKYG NKQELKSLVA AFREQGVKSI SDIVINHRTA 120 ERLDNNGLSI FEGGTPDNRL DWDVSYICGN DVQFKGTGNN DTGDDWGGAP DVDHTNPKVQ 180 QELSDWMNWF TKNYVEKTSP DFTVGELYRN VELGSDGKPL ANQDKHRETL VKWVNDAGGV 240 VTTFDFTTKM ILGAAVQGEL WRMKDANGKP PGMIGIMPSN AVTFVDNHDT GSQKLWPFPD 300 DKVMLGYVYI LTHPGHPTIF YDHYIEWGLM EPIKKLTAIR KRNGITATSN VNILAAENDL 360 YMANIGNKII VKIGPKLDLG NLLPPNAQVA TSGQDYAVWE IK* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00810 | Alpha-amyl_C2 | 4.0e-27 | 341 | 400 | 60 | + Alpha-amylase C-terminal beta-sheet domain. This entry represents the beta-sheet domain that is found in several alpha-amylases, usually at the C-terminus. This domain is organised as a five-stranded anti-parallel beta-sheet. | ||
PLN02784 | PLN02784 | 2.0e-103 | 28 | 402 | 403 | + alpha-amylase | ||
PLN02361 | PLN02361 | 4.0e-110 | 28 | 400 | 403 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-118 | 28 | 351 | 347 | + 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 | 9.0e-162 | 28 | 400 | 400 | + 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:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PRF/SEQDB | 0 | 1 | 400 | 1 | 421 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
DDBJ | BAA33879.1 | 0 | 1 | 400 | 1 | 420 | alpha-amylase [Phaseolus vulgaris] |
DDBJ | BAC76729.1 | 0 | 1 | 400 | 1 | 421 | alpha-amylase [Vigna angularis] |
Swiss-Prot | P17859 | 0 | 1 | 400 | 1 | 421 | AMYA_VIGMU RecName: Full=Alpha-amylase; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; Flags: Precursor |
RefSeq | XP_002282184.1 | 0 | 1 | 402 | 1 | 425 | 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 | 25 | 400 | 2 | 401 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1ava_B | 0 | 25 | 400 | 2 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 25 | 400 | 2 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 25 | 400 | 2 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 25 | 400 | 3 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |