| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.002G132300.1 |
| Family | GH13 |
| Protein Properties | Length: 416 Molecular Weight: 46334.1 Isoelectric Point: 4.7013 |
| Chromosome | Chromosome/Scaffold: 02 Start: 20736799 End: 20738651 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH13 | 32 | 334 | 2.79979e-42 |
| SSNKAGGWYNFLQSSVSDISNAGVTHVWLPPPSQSAAPQGYLPGRLYDLDASKYGSQAELKSLIDAFHQKGVKCVADIVINHRTAERQDNRGIYCLFEGG TSDDRLDWGPSFICKDDTAYSDGTGNPDTGLPYDPAPDIDHLNPRVQNELSDWLNWLKTEIGFDGWRFDFVRGYAPTITKIYMDRTSPDFAVGEKWEDFI DGQEDLHRAALKDWVEAAGGAVTAFDFTTKGVLNDAVQGKLWRLKDSSGKPPGMIGLLPQNAVTFIDNHDTGSTQNIWPFPSDKIMQGYAYILTHPGIPS IFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 416 Download |
| MLTSLCFVFI FIFVFSPFAT PTLLFQGFNW ESSNKAGGWY NFLQSSVSDI SNAGVTHVWL 60 PPPSQSAAPQ GYLPGRLYDL DASKYGSQAE LKSLIDAFHQ KGVKCVADIV INHRTAERQD 120 NRGIYCLFEG GTSDDRLDWG PSFICKDDTA YSDGTGNPDT GLPYDPAPDI DHLNPRVQNE 180 LSDWLNWLKT EIGFDGWRFD FVRGYAPTIT KIYMDRTSPD FAVGEKWEDF IDGQEDLHRA 240 ALKDWVEAAG GAVTAFDFTT KGVLNDAVQG KLWRLKDSSG KPPGMIGLLP QNAVTFIDNH 300 DTGSTQNIWP FPSDKIMQGY AYILTHPGIP SIFYDHFFDL GLKDEISKLV EIRNRNGIQS 360 TSTVTIRASE SELYMASIDD KIIMKIGPKM DLGNLVPPNY QLATSGNNYA VWEKK* 420 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-51 | 24 | 355 | 400 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 3.0e-136 | 23 | 415 | 404 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 3.0e-143 | 23 | 414 | 404 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-161 | 24 | 364 | 344 | + 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 | 4 | 414 | 421 | + 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 | 2 | 413 | 4 | 421 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
| DDBJ | BAC76729.1 | 0 | 2 | 413 | 4 | 421 | alpha-amylase [Vigna angularis] |
| Swiss-Prot | P17859 | 0 | 2 | 413 | 4 | 421 | AMYA_VIGMU RecName: Full=Alpha-amylase; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; Flags: Precursor |
| RefSeq | XP_002301187.1 | 0 | 22 | 415 | 4 | 404 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002327139.1 | 0 | 4 | 414 | 5 | 423 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 23 | 414 | 2 | 402 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 1ava_B | 0 | 23 | 414 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 23 | 414 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 23 | 414 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 23 | 414 | 3 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
