| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G138468_T01 |
| Family | GH13 |
| Protein Properties | Length: 440 Molecular Weight: 48269.2 Isoelectric Point: 6.2219 |
| Chromosome | Chromosome/Scaffold: 2 Start: 186265525 End: 186267387 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 44 | 348 | 6.20005e-41 |
| GGWYNYLLGRVDDIAATGATHVWLPPPSHSVAPQGYMPGRLYDLDASKYGTHAELKSLTAAFHAKGVQCVADVVINHRCADYKDGRGIYCVFEGGTPDSR LDWGPDMICSDDTQYSNGRGHRDTGADFAAAPDIDHLNPRVQQELSDWLNWLKSDLGFDGWRLDFAKGYSAAVAKVYVDSTAPTFVVAEIWSSLHYDGNG EPSSNQDADRQELVNWAQAVGGPAAAFDFTTKGVLQAAVQGELWRMKDGNGKAPGMIGWLPEKAVTFVDNHDTGSTQNSWPFPSDKVMQGYAYILTHPGT PCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 440 Download |
| MAKHLAAMCR CSLLVLVLLC LGSQLAQSQV LFQGFNWESW KKQGGWYNYL LGRVDDIAAT 60 GATHVWLPPP SHSVAPQGYM PGRLYDLDAS KYGTHAELKS LTAAFHAKGV QCVADVVINH 120 RCADYKDGRG IYCVFEGGTP DSRLDWGPDM ICSDDTQYSN GRGHRDTGAD FAAAPDIDHL 180 NPRVQQELSD WLNWLKSDLG FDGWRLDFAK GYSAAVAKVY VDSTAPTFVV AEIWSSLHYD 240 GNGEPSSNQD ADRQELVNWA QAVGGPAAAF DFTTKGVLQA AVQGELWRMK DGNGKAPGMI 300 GWLPEKAVTF VDNHDTGSTQ NSWPFPSDKV MQGYAYILTH PGTPCIFYDH VFDWNLKQEI 360 SALSAVRSRN GIHPGSELNI LAADGDLYVA KIDDKVIVKI GSRYDVGNLI PSDFHAVAHG 420 NNYCVWEKHG LRVPAGRHH* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 3.0e-42 | 27 | 348 | 386 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02361 | PLN02361 | 6.0e-140 | 29 | 428 | 405 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 5.0e-142 | 29 | 428 | 401 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-160 | 30 | 378 | 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 | 26 | 428 | 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 |
| GenBank | ACF88424.1 | 0 | 1 | 439 | 1 | 439 | unknown [Zea mays] |
| GenBank | EAZ09376.1 | 0 | 1 | 439 | 1 | 437 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
| RefSeq | NP_001063369.1 | 0 | 1 | 439 | 1 | 437 | Os09g0457800 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001105539.1 | 0 | 1 | 439 | 1 | 439 | alpha-amylase [Zea mays] |
| RefSeq | XP_002460331.1 | 0 | 1 | 439 | 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 | 29 | 428 | 1 | 402 | A Chain A, Class Iv Chitinase Structure From Picea Abies At 1.8a |
| PDB | 1ava_B | 0 | 29 | 428 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 29 | 428 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 29 | 428 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 3bsg_A | 0 | 29 | 430 | 2 | 406 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
