| Basic Information | |
|---|---|
| Species | Panicum virgatum |
| Cazyme ID | Pavirv00011095m |
| Family | GH13 |
| Protein Properties | Length: 438 Molecular Weight: 48115.9 Isoelectric Point: 6.1053 |
| Chromosome | Chromosome/Scaffold: 085372 Start: 459 End: 2194 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 42 | 346 | 1.3e-40 |
| GGWYNYLRGQVDDIAATGATLVWLPPPSHSVAPQGYMPGRLYDLDASKYGTHADLKSLIAAFHAKGVQCVADIVINHRCADYKDSRGIYCVFEGGTPDGR LDWGPDMICSDDTQYSNGRGHRDTGADFGAAPDIDHLNPRIQQELSDWLNWLKSDLGFDGWRLDFAKGYSAAVAKVYVDNTAPTFVVAEIWSSLQYDGNG EPSSNQDRDRQELVNWAQSVGGPAAAFDFTTKGVLQSAVQGELWRLKDGNGKAPGMIGWLPEKAVTFVDNHDTGSTQNSWPFPSDKVVQGYAYILTHPGT PCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 438 Download |
| MTKHSAAMCS LLVLVLLGLG SQLVQSQVLF QGFNWESWKK QGGWYNYLRG QVDDIAATGA 60 TLVWLPPPSH SVAPQGYMPG RLYDLDASKY GTHADLKSLI AAFHAKGVQC VADIVINHRC 120 ADYKDSRGIY CVFEGGTPDG RLDWGPDMIC SDDTQYSNGR GHRDTGADFG AAPDIDHLNP 180 RIQQELSDWL NWLKSDLGFD GWRLDFAKGY SAAVAKVYVD NTAPTFVVAE IWSSLQYDGN 240 GEPSSNQDRD RQELVNWAQS VGGPAAAFDF TTKGVLQSAV QGELWRLKDG NGKAPGMIGW 300 LPEKAVTFVD NHDTGSTQNS WPFPSDKVVQ GYAYILTHPG TPCIFYDHVF DWNLKQEISV 360 LSAVRSRNGI HPGSKLDILA ADGDLYVAKI DDKVIVKIGS RYDVGNLIPS DFHPVAHGNN 420 YCVWERSGLR VPAGRHH* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| PRK09441 | PRK09441 | 2.0e-42 | 42 | 346 | 371 | + cytoplasmic alpha-amylase; Reviewed |
| PLN02361 | PLN02361 | 3.0e-133 | 34 | 426 | 398 | + alpha-amylase |
| PLN02784 | PLN02784 | 6.0e-134 | 34 | 427 | 395 | + alpha-amylase |
| cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-153 | 34 | 376 | 346 | + 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 | 34 | 426 | 396 | + 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 |
| GenBank | ACF88424.1 | 0 | 1 | 437 | 1 | 439 | unknown [Zea mays] |
| GenBank | EAZ09376.1 | 0 | 1 | 437 | 1 | 437 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
| RefSeq | NP_001063369.1 | 0 | 1 | 437 | 1 | 437 | Os09g0457800 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001105539.1 | 0 | 1 | 437 | 1 | 439 | alpha-amylase [Zea mays] |
| RefSeq | XP_002460331.1 | 0 | 1 | 437 | 1 | 437 | hypothetical protein SORBIDRAFT_02g026610 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 27 | 426 | 1 | 402 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 1ava_B | 0 | 27 | 426 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 27 | 426 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 27 | 426 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1rpk_A | 0 | 27 | 427 | 2 | 405 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| 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 |
