| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 97625 |
| Family | GH13 |
| Protein Properties | Length: 408 Molecular Weight: 46076.4 Isoelectric Point: 4.6113 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 30 | 324 | 2e-40 |
| DLAQAGVTDIWLPPATHSVAPQGYMPGRLYDLNASKYGNEEKLKQVIDKFHSHGIRCIADIVINHRCGDSQDQRGVWCIFEGGTPDERLDWGPWAITKDD YAYSDGSGAPDTGEDFGAAPDIDHTNPRVQDDLAGWMKWMKETIGFDGWRFDFSKGYAGSYTGLYIERTTPEFSVGEFWTNLNYGPDGSVEYNQDSHRQE VVDWINATGNRSTAFDFTTKGILQEAVKNQFWRLRDPNNKPAGVIGYWPQKAVTFVDNHDTGSTQKHWPFPADKVMLGYVYILTHPGIPCIFYDH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 408 Download |
| MIFCVAFQGF NWESWRNPCW YDVLMNTAED LAQAGVTDIW LPPATHSVAP QGYMPGRLYD 60 LNASKYGNEE KLKQVIDKFH SHGIRCIADI VINHRCGDSQ DQRGVWCIFE GGTPDERLDW 120 GPWAITKDDY AYSDGSGAPD TGEDFGAAPD IDHTNPRVQD DLAGWMKWMK ETIGFDGWRF 180 DFSKGYAGSY TGLYIERTTP EFSVGEFWTN LNYGPDGSVE YNQDSHRQEV VDWINATGNR 240 STAFDFTTKG ILQEAVKNQF WRLRDPNNKP AGVIGYWPQK AVTFVDNHDT GSTQKHWPFP 300 ADKVMLGYVY ILTHPGIPCI FYDHYYEWGL KDEIKALLEV RKRNNVVANS SVSIIAAEED 360 VYVASVADGK LVVKMGPRFD IGDMAPSSDE FAIAALGNEY CVWERKN* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| PRK09441 | PRK09441 | 5.0e-45 | 5 | 343 | 413 | + cytoplasmic alpha-amylase; Reviewed |
| PLN02784 | PLN02784 | 2.0e-137 | 3 | 406 | 405 | + alpha-amylase |
| PLN02361 | PLN02361 | 3.0e-156 | 5 | 405 | 404 | + alpha-amylase |
| cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-171 | 5 | 352 | 351 | + 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 | 5 | 405 | 405 | + alpha-amylase; Provisional |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAC02435.1 | 0 | 5 | 406 | 24 | 423 | alpha-amylase [Ipomoea nil] |
| RefSeq | XP_001754460.1 | 0 | 9 | 407 | 1 | 397 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001777583.1 | 0 | 9 | 405 | 16 | 410 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002282184.1 | 0 | 5 | 406 | 25 | 425 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002301187.1 | 0 | 1 | 406 | 1 | 404 | 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 | 5 | 405 | 2 | 402 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
| PDB | 1ava_B | 0 | 5 | 405 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 5 | 405 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 5 | 405 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 5 | 405 | 3 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO476908 | 401 | 5 | 405 | 0 |
| HO409542 | 408 | 2 | 408 | 0 |
| HO420508 | 403 | 5 | 406 | 0 |
| FE452335 | 241 | 117 | 357 | 0 |
| FD743295 | 295 | 34 | 327 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
