y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.014G029400.1 |
Family | GH13 |
Protein Properties | Length: 424 Molecular Weight: 46830.4 Isoelectric Point: 4.6765 |
Chromosome | Chromosome/Scaffold: 14 Start: 2493741 End: 2495748 |
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 | 32 | 343 | 3.50002e-41 |
ESCNKAGGWYNSLKNSVPDLANAGITHVWLPPSSQSVAPQGRYMPGRLYDLSASRYGSQDELKSLIGDFNQKGIKCLADIVINHRTAEKQDERGIWSVFE GGTSDGRLDWGPSFICGDDTAYSDGKGNPDSGDDFEPAPDIDHLNPRVQRELSDWMNWLKSEIGFDGWRFDFVKGYAPSVTKIYMENTSPDFAVGEKWDS LAYGQDGKLDYNQDAHRGSIKDWIQAAGGAVTAFDFTSKGILQAAVQGELWRLKDSNGKPPGLIGLLPQNAVTFIDNHDTGSTQQIWPFPSDKVMQGYAY ILTHPGTPSIFY |
Full Sequence |
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Protein Sequence Length: 424 Download |
MSFLTFCFFS LFLSVFPLLT SSYLLFQGFN WESCNKAGGW YNSLKNSVPD LANAGITHVW 60 LPPSSQSVAP QGRYMPGRLY DLSASRYGSQ DELKSLIGDF NQKGIKCLAD IVINHRTAEK 120 QDERGIWSVF EGGTSDGRLD WGPSFICGDD TAYSDGKGNP DSGDDFEPAP DIDHLNPRVQ 180 RELSDWMNWL KSEIGFDGWR FDFVKGYAPS VTKIYMENTS PDFAVGEKWD SLAYGQDGKL 240 DYNQDAHRGS IKDWIQAAGG AVTAFDFTSK GILQAAVQGE LWRLKDSNGK PPGLIGLLPQ 300 NAVTFIDNHD TGSTQQIWPF PSDKVMQGYA YILTHPGTPS IFYDHFFDWG LKEEIGKLAT 360 IRKNYGIGSA STVNILASDA DLYVAAINDN IIMKIGPKTD LGNLIPSNFQ VATSGTDYCV 420 WVK* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 5.0e-50 | 25 | 385 | 433 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02361 | PLN02361 | 2.0e-147 | 24 | 423 | 405 | + alpha-amylase | ||
PLN02784 | PLN02784 | 6.0e-148 | 24 | 421 | 399 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-160 | 25 | 373 | 352 | + 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 | 24 | 423 | 403 | + 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 | 2 | 421 | 3 | 420 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
DDBJ | BAC76729.1 | 0 | 2 | 421 | 3 | 420 | alpha-amylase [Vigna angularis] |
RefSeq | XP_002301187.1 | 0 | 24 | 423 | 5 | 403 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002327139.1 | 0 | 1 | 423 | 1 | 423 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510218.1 | 0 | 4 | 423 | 1 | 420 | 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 | 24 | 423 | 2 | 402 | A Chain A, Crystal Structure Of Nxg1-Deltayniig In Complex With Xllg, A Xyloglucan Derived Oligosaccharide |
PDB | 1ava_B | 0 | 24 | 423 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 24 | 423 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 24 | 423 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 24 | 423 | 3 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1823 | EC-3.2.1.1 | α-amylase |
starch degradation I | RXN-1825 | EC-3.2.1.1 | α-amylase |