Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si013755m |
Family | GH13 |
Protein Properties | Length: 442 Molecular Weight: 48229.3 Isoelectric Point: 6.6746 |
Chromosome | Chromosome/Scaffold: 6 Start: 30612863 End: 30614824 |
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 | 51 | 350 | 3.39955e-42 |
LKVQVDDIANAGATHVWLPPPSHSVAPQGYMPGRLYDLNASRYGTEAELRSLIAAFRGRGIQAVADVVINHRCADKQDARGVYCVFEGGDPEGRRLNWDA DMICSDDTAYSNGRGNRDTGKDFGAAPDIDHLNPRVRRELTDWLRWLTADVGFGGWRLDFAKGYSAAVAKAYVDGAGPSFVVAEIWSSLNYDGDGKPANN QDGDRQELVDWANAVGGPAAAFDFTTKGVLQAAVQGELWRMRDGNGKAPGLIGWLPEKAVTFIDNHDTGSTQNSWPFPRDKVMQGYAYILTHPGIPCIFY |
Full Sequence |
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Protein Sequence Length: 442 Download |
MTRPHLPVLF GLLVVTAALG LLGSNTARAQ VLFQGFNWES CKNQGGWYNN LKVQVDDIAN 60 AGATHVWLPP PSHSVAPQGY MPGRLYDLNA SRYGTEAELR SLIAAFRGRG IQAVADVVIN 120 HRCADKQDAR GVYCVFEGGD PEGRRLNWDA DMICSDDTAY SNGRGNRDTG KDFGAAPDID 180 HLNPRVRREL TDWLRWLTAD VGFGGWRLDF AKGYSAAVAK AYVDGAGPSF VVAEIWSSLN 240 YDGDGKPANN QDGDRQELVD WANAVGGPAA AFDFTTKGVL QAAVQGELWR MRDGNGKAPG 300 LIGWLPEKAV TFIDNHDTGS TQNSWPFPRD KVMQGYAYIL THPGIPCIFY DHVFDWNLKE 360 EISTLAAIRK RNGIHPGSKL SILKAEGDVY VAMIDDKVIT KIGPRYDVGG VIPSGFHVAA 420 PGEGYCVWEK SGLRVPSGRY R* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 3.0e-50 | 28 | 371 | 416 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 3.0e-150 | 30 | 431 | 403 | + alpha-amylase | ||
PLN02361 | PLN02361 | 3.0e-155 | 30 | 430 | 406 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-164 | 31 | 380 | 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 | 24 | 430 | 410 | + alpha-amylase; Provisional |
Gene Ontology | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | EAZ09376.1 | 0 | 23 | 439 | 20 | 435 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
RefSeq | NP_001063368.1 | 0 | 25 | 441 | 22 | 437 | Os09g0457600 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001063369.1 | 0 | 23 | 439 | 20 | 435 | Os09g0457800 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002444507.1 | 0 | 25 | 430 | 26 | 437 | hypothetical protein SORBIDRAFT_07g023010 [Sorghum bicolor] |
RefSeq | XP_002460331.1 | 0 | 23 | 441 | 20 | 437 | hypothetical protein SORBIDRAFT_02g026610 [Sorghum bicolor] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1bg9_A | 0 | 30 | 430 | 1 | 402 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1ava_B | 0 | 30 | 430 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 30 | 430 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 30 | 430 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 30 | 432 | 2 | 406 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
Metabolic Pathways | |||
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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 |