| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os09g28420.1 |
| Family | GH13 |
| Protein Properties | Length: 438 Molecular Weight: 48333.2 Isoelectric Point: 6.1891 |
| Chromosome | Chromosome/Scaffold: 9 Start: 17296166 End: 17305076 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 42 | 346 | 5.79997e-42 |
| GGWYNFLHGHVDDIAATGVTHVWLPPPSHSVAPQGYMPGRLYDLDASKYGTGAELRSLIAAFHSKGIKCVADIVINHRCADYKDSRGIYCIFEGGTPDSR LDWGPDMICSDDTQYSNGRGHRDTGADFGAAPDIDHLNTRVQTELSDWLNWLKSDVGFDGWRLDFAKGYSAAVAKTYVDNTDPSFVVAEIWSNMRYDGNG EPSWNQDGDRQELVNWAQAVGGPASAFDFTTKGELQAAVQGELWRMKDGNGKAPGMIGWLPEKAVTFIDNHDTGSTQNSWPFPSDKVMQGYAYILTHPGV PCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 438 Download |
| MAKRIASMSS LLLIALLCLS SHLAQAQVLF QGFNWESWKK QGGWYNFLHG HVDDIAATGV 60 THVWLPPPSH SVAPQGYMPG RLYDLDASKY GTGAELRSLI AAFHSKGIKC VADIVINHRC 120 ADYKDSRGIY CIFEGGTPDS RLDWGPDMIC SDDTQYSNGR GHRDTGADFG AAPDIDHLNT 180 RVQTELSDWL NWLKSDVGFD GWRLDFAKGY SAAVAKTYVD NTDPSFVVAE IWSNMRYDGN 240 GEPSWNQDGD RQELVNWAQA VGGPASAFDF TTKGELQAAV QGELWRMKDG NGKAPGMIGW 300 LPEKAVTFID NHDTGSTQNS WPFPSDKVMQ GYAYILTHPG VPCIFYDHVF DWNLKQEIST 360 LAAVRSRNGI HPGSKLNILA ADGDVYVAMI DDKVITKIGT RYDVGNLIPS DFHVVAHGNN 420 YCVWEKSGLR VPAGRRH* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00810 | Alpha-amyl_C2 | 4.0e-33 | 366 | 426 | 61 | + Alpha-amylase C-terminal beta-sheet domain. This entry represents the beta-sheet domain that is found in several alpha-amylases, usually at the C-terminus. This domain is organised as a five-stranded anti-parallel beta-sheet. | ||
| PLN02361 | PLN02361 | 7.0e-139 | 27 | 426 | 405 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 2.0e-141 | 27 | 427 | 402 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-158 | 28 | 376 | 352 | + 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 | 27 | 426 | 403 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005576 | extracellular region |
| 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 |
| EMBL | CAA39778.1 | 0 | 1 | 437 | 1 | 437 | alpha-amylase [Oryza sativa (japonica cultivar-group)] |
| GenBank | EAZ09376.1 | 0 | 1 | 437 | 1 | 437 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
| RefSeq | NP_001063368.1 | 0 | 1 | 437 | 1 | 437 | Os09g0457600 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001063369.1 | 0 | 1 | 437 | 1 | 437 | Os09g0457800 [Oryza sativa (japonica cultivar-group)] |
| 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, 3.0 A Structure Of The Prunus Mume Hydroxynitrile Lyase Isozyme-1 |
| 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 |
