| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb07g023020.1 |
| Family | GH13 |
| Protein Properties | Length: 439 Molecular Weight: 48258.8 Isoelectric Point: 6.619 |
| Chromosome | Chromosome/Scaffold: 7 Start: 57874031 End: 57875893 |
| 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 | 41 | 347 | 9.49996e-41 |
| PGGWYNRLKAQVDDIANAGVTHVWLPPPSHSVSPQGYMPGRLYDLDASKYGTAAELRSLIAAFHGRRIQCVADIVINHRCAEKKDARGIYCIFEGGTGDG RLDWGPGMICSDDTEYSDGTGHRDTGEAFAAAPDVDHLNERVRRELSAWLNWLKSDDVGFDGWRLDFAKGYSPAVARMYVESTAPSFVVAEIWNSLTLSG DGKPSPNQDQCRQELVNWVQAVGGPAMAFDFTTKGLLQAGVQGELWRLRDSSGKAAGMIGWMPEKAVTFVDNHDTGSTQKLWPFPSDKVMQGYAYILTHP GVPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 439 Download |
| MKHSSSLCLL FLVALCISLA CGLVQAQVLF QGFNWESCKQ PGGWYNRLKA QVDDIANAGV 60 THVWLPPPSH SVSPQGYMPG RLYDLDASKY GTAAELRSLI AAFHGRRIQC VADIVINHRC 120 AEKKDARGIY CIFEGGTGDG RLDWGPGMIC SDDTEYSDGT GHRDTGEAFA AAPDVDHLNE 180 RVRRELSAWL NWLKSDDVGF DGWRLDFAKG YSPAVARMYV ESTAPSFVVA EIWNSLTLSG 240 DGKPSPNQDQ CRQELVNWVQ AVGGPAMAFD FTTKGLLQAG VQGELWRLRD SSGKAAGMIG 300 WMPEKAVTFV DNHDTGSTQK LWPFPSDKVM QGYAYILTHP GVPCIFYDHM FDWNLKQEIS 360 TLSAIRARNG IHAGSKLRIL VADADAYVAV VDEKVMVKIG TRYDVSNVIP SDFHPAAHGK 420 DYCVWEKGSL RVPAGRHL* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 1.0e-47 | 25 | 369 | 417 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 5.0e-131 | 27 | 427 | 402 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 4.0e-134 | 27 | 427 | 405 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-162 | 28 | 377 | 353 | + 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 | 427 | 427 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PIR | 0 | 20 | 438 | 19 | 435 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
| GenBank | AAA33895.1 | 0 | 20 | 438 | 19 | 435 | alpha-amylase [Oryza sativa Japonica Group] |
| GenBank | ACN34260.1 | 0 | 22 | 438 | 24 | 441 | unknown [Zea mays] |
| RefSeq | NP_001062024.1 | 0 | 20 | 438 | 59 | 476 | Os08g0473900 [Oryza sativa (japonica cultivar-group)] |
| Swiss-Prot | P27933 | 0 | 20 | 438 | 19 | 436 | AMY3D_ORYSJ RecName: Full=Alpha-amylase isozyme 3D; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; Flags: Precursor |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1rpk_A | 0 | 27 | 427 | 2 | 404 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1p6w_A | 0 | 27 | 427 | 2 | 404 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ht6_A | 0 | 27 | 427 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 2qpu_C | 0 | 27 | 427 | 2 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 27 | 427 | 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 |
