| Basic Information | |
|---|---|
| Species | Setaria italica |
| Cazyme ID | Si027629m |
| Family | GH13 |
| Protein Properties | Length: 426 Molecular Weight: 46812.8 Isoelectric Point: 5.9219 |
| Chromosome | Chromosome/Scaffold: 8 Start: 32503779 End: 32505234 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH13 | 48 | 346 | 2.50006e-41 |
| SSQVDAIAGAGITHVWLPPPSHSVDARGYLPGRLYDLNVSRYGNETQLRALVAAFHRRGIKCVADVVLNHRTAERKDGRGVYCIFEGGTPDGRLDWGPHM LCRNDSYSDGTGNADTGLDYQPAPDLDHLNARVRSELADWLNWLKADVGFDGWRLDFANGYSPAVAGMYINATSPDLAAAEIWTDLAYEADGKPRANQDA HRQILAAWVDAVGGPAAAFDYTTKGVLQAALNFSELWRMQDAQGRAPGLVGLRPAQSVTFVDNHDTGSKTQHSWPFPPEKVLQGYAYILSHPGIPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 426 Download |
| MRKSQVCLLL FLVILGSLSQ SALSQILLQA FNWESCSQGG SGWYDLLSSQ VDAIAGAGIT 60 HVWLPPPSHS VDARGYLPGR LYDLNVSRYG NETQLRALVA AFHRRGIKCV ADVVLNHRTA 120 ERKDGRGVYC IFEGGTPDGR LDWGPHMLCR NDSYSDGTGN ADTGLDYQPA PDLDHLNARV 180 RSELADWLNW LKADVGFDGW RLDFANGYSP AVAGMYINAT SPDLAAAEIW TDLAYEADGK 240 PRANQDAHRQ ILAAWVDAVG GPAAAFDYTT KGVLQAALNF SELWRMQDAQ GRAPGLVGLR 300 PAQSVTFVDN HDTGSKTQHS WPFPPEKVLQ GYAYILSHPG IPCIFYDHFF DPTMKDEIAT 360 MIKIRTRDKI GPTSSLRILL AQHDAYVAEI DGKVVAKVGA RYDVSKIVPP EFVVTTSGND 420 FAIWEN |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-38 | 31 | 365 | 402 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02361 | PLN02361 | 1.0e-118 | 31 | 425 | 399 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 4.0e-123 | 31 | 425 | 395 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-141 | 31 | 376 | 348 | + 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 | 31 | 425 | 399 | + 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 |
| PDB | 3BSG | 0 | 25 | 426 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| GenBank | AAA98615.1 | 0 | 1 | 426 | 1 | 426 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
| GenBank | AAM09952.1 | 0 | 25 | 426 | 1 | 402 | alpha-amylase [Eleusine coracana subsp. coracana] |
| RefSeq | XP_002452881.1 | 0 | 1 | 426 | 1 | 427 | hypothetical protein SORBIDRAFT_04g034150 [Sorghum bicolor] |
| RefSeq | XP_002460139.1 | 0 | 19 | 426 | 19 | 427 | hypothetical protein SORBIDRAFT_02g023250 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3bsg_A | 0 | 25 | 426 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 25 | 426 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1p6w_A | 0 | 25 | 426 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1ht6_A | 0 | 25 | 426 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 2qpu_C | 0 | 25 | 426 | 2 | 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 |
