Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna28571.1-v1.0-hybrid |
Family | GH13 |
Protein Properties | Length: 411 Molecular Weight: 45539.9 Isoelectric Point: 4.8348 |
Chromosome | Chromosome/Scaffold: 3 Start: 21103754 End: 21106489 |
Description | alpha-amylase-like |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 38 | 328 | 3.69999e-41 |
KGGWYNILEQSAAELASSGITHVWLPPPSQSVSDEGYMPGRLYDLTSKYGNQDELKALVKAYHDKGIQSIADIVINHRCAEKQDERGKWCIFEGGTPDDR LDWGPSLICSDDTDYSDGKGNPDTGAPFVPAPDIDHKNTRVQSELSDWMNWLKTEIGFSGWRFDFVMGYAPEFTKLYVANTKPSFSVGEYWNSTTRDELA GWIGNAGGEVTAFDFTTKGILQAAVQGELWRLKDSNGGPPGLIGILPRNSVTFIDNHDTGSTQKKWEFPSDKVMQGYAYTLTHPGVPSIFY |
Full Sequence |
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Protein Sequence Length: 411 Download |
MKPPKSEIED SVKYSMEVHP EMKLNKSLEG FNWESARKGG WYNILEQSAA ELASSGITHV 60 WLPPPSQSVS DEGYMPGRLY DLTSKYGNQD ELKALVKAYH DKGIQSIADI VINHRCAEKQ 120 DERGKWCIFE GGTPDDRLDW GPSLICSDDT DYSDGKGNPD TGAPFVPAPD IDHKNTRVQS 180 ELSDWMNWLK TEIGFSGWRF DFVMGYAPEF TKLYVANTKP SFSVGEYWNS TTRDELAGWI 240 GNAGGEVTAF DFTTKGILQA AVQGELWRLK DSNGGPPGLI GILPRNSVTF IDNHDTGSTQ 300 KKWEFPSDKV MQGYAYTLTH PGVPSIFYDH FFDWGLKGEI SNLTAIRSRN GIKPDSAVSI 360 LAADADLYVA SIDDKIITKI GPRFDVGNLV PSTFKIATSG KDYCVWEKSA * 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 9.0e-45 | 31 | 349 | 391 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 5.0e-125 | 28 | 409 | 396 | + alpha-amylase | ||
PLN02361 | PLN02361 | 2.0e-125 | 28 | 408 | 400 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-141 | 28 | 358 | 341 | + 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 | 28 | 408 | 400 | + 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 - 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 | 28 | 408 | 4 | 402 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1ava_B | 0 | 28 | 408 | 4 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 28 | 408 | 4 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 28 | 408 | 4 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 28 | 409 | 5 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
Sequence Alignments (This image is cropped. Click for full image.) |
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