| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G070172_T01 |
| Family | GH13 |
| Protein Properties | Length: 442 Molecular Weight: 48415.9 Isoelectric Point: 6.8232 |
| Chromosome | Chromosome/Scaffold: 1 Start: 199630232 End: 199632219 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 49 | 350 | 4.90454e-43 |
| RLKAQVDDIAKAGVTHVWLPPPSHSVSPQGYMPGRLYDLDASKYGTAAELKSLIAAFHGRGVQCVADIVINHRCAEKKDARGVYCIFEGGTPDDRLDWGP GMICSDDTQYSDGTGHRDTGEGFAAAPDIDHLNPRVQRELSAWLNWLRSDAVGFDGWRLDFAKGYSPAVARMYVESTGPPSFVVAEIWNSLSYSGDGKPA PNQDQCRQELLDWTRAVGGPAMAFDFPTKGLLQAGVQGELWRLRDSSGNAAGLIGWAPEKAVTFVDNHDTGSTQKLWPFPSDKVMQGYAYILTHPGVPCI FY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 442 Download |
| MMKHSSSLCL LFLLALCTTL LACGLVQAQV LFQGFNWESC KQQGGWYNRL KAQVDDIAKA 60 GVTHVWLPPP SHSVSPQGYM PGRLYDLDAS KYGTAAELKS LIAAFHGRGV QCVADIVINH 120 RCAEKKDARG VYCIFEGGTP DDRLDWGPGM ICSDDTQYSD GTGHRDTGEG FAAAPDIDHL 180 NPRVQRELSA WLNWLRSDAV GFDGWRLDFA KGYSPAVARM YVESTGPPSF VVAEIWNSLS 240 YSGDGKPAPN QDQCRQELLD WTRAVGGPAM AFDFPTKGLL QAGVQGELWR LRDSSGNAAG 300 LIGWAPEKAV TFVDNHDTGS TQKLWPFPSD KVMQGYAYIL THPGVPCIFY DHMFDWNLKQ 360 EISTLSAIRA RNGIRAGSKL RILVADADAY VAVVDEKVMV KIGTRYGVSS VVPSDFHPAA 420 HGKDYCVWEK ASLRVPAGRH L* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 8.0e-52 | 27 | 372 | 427 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 2.0e-126 | 29 | 431 | 404 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 2.0e-129 | 29 | 430 | 407 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-159 | 30 | 380 | 354 | + 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 | 29 | 431 | 406 | + 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 |
| PIR | 0 | 22 | 441 | 19 | 435 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
| GenBank | AAA33895.1 | 0 | 22 | 441 | 19 | 435 | alpha-amylase [Oryza sativa Japonica Group] |
| GenBank | ACN34260.1 | 0 | 1 | 441 | 1 | 441 | unknown [Zea mays] |
| RefSeq | NP_001062024.1 | 0 | 22 | 441 | 59 | 476 | Os08g0473900 [Oryza sativa (japonica cultivar-group)] |
| Swiss-Prot | P27933 | 0 | 22 | 441 | 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 | 29 | 430 | 2 | 404 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 1p6w_A | 0 | 29 | 430 | 2 | 404 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 1ht6_A | 0 | 29 | 430 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 2qpu_C | 0 | 29 | 430 | 2 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 29 | 430 | 2 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
