Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00065049m |
Family | GH13 |
Protein Properties | Length: 399 Molecular Weight: 45598.2 Isoelectric Point: 5.9859 |
Chromosome | Chromosome/Scaffold: 0119114 Start: 91 End: 3319 |
Description | alpha-amylase-like 2 |
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 | 31 | 318 | 1.5e-32 |
KVTDLAESGFTSAWLPPPTQSLSREGYLPQNLYCLDSCYGSLSELKSLLHKMNEHNLRAMADVVINHRIGTTQGSNGMYNRYDGIPISWDEHAVTSCSGG KGNKSTGDNFDGVPNIDHTQTFVRKDIIEWLIWLRISVGFQDFRFDFTKGYAAKFVKEYIEESKPLFAVGEYWDSCEYSPPDYRLNYNQDNHRQRIINWI DSTGGLCAAFDFTTKGILQEAVKGELWRLRDPEGKPPGVMGWWPSRSVTFIENHDTGSTQGHWPFPSDHIMEGYAYILTHPGIPAVFY |
Full Sequence |
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Protein Sequence Length: 399 Download |
GGIIKNGREI LFQAFNWESN KHNWWSMLEE KVTDLAESGF TSAWLPPPTQ SLSREGYLPQ 60 NLYCLDSCYG SLSELKSLLH KMNEHNLRAM ADVVINHRIG TTQGSNGMYN RYDGIPISWD 120 EHAVTSCSGG KGNKSTGDNF DGVPNIDHTQ TFVRKDIIEW LIWLRISVGF QDFRFDFTKG 180 YAAKFVKEYI EESKPLFAVG EYWDSCEYSP PDYRLNYNQD NHRQRIINWI DSTGGLCAAF 240 DFTTKGILQE AVKGELWRLR DPEGKPPGVM GWWPSRSVTF IENHDTGSTQ GHWPFPSDHI 300 MEGYAYILTH PGIPAVFYDH FYDQGLSLHD EIVKLMQIRK CQDIHSRSSV KILEAKSDLY 360 SAIIDEKLCM KIGDGSWCPS EPEWRLAASG DRYAVWHK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-41 | 6 | 340 | 418 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 5.0e-143 | 9 | 398 | 406 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-157 | 10 | 350 | 345 | + 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. | ||
PLN02784 | PLN02784 | 6.0e-168 | 6 | 398 | 400 | + alpha-amylase | ||
PLN02361 | PLN02361 | 0 | 1 | 398 | 398 | + alpha-amylase |
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 |
EMBL | CAE02023.2 | 0 | 1 | 398 | 15 | 412 | OSJNBb0118P14.5 [Oryza sativa (japonica cultivar-group)] |
EMBL | CAX51375.1 | 0 | 2 | 398 | 19 | 415 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
RefSeq | NP_001052697.1 | 0 | 1 | 398 | 47 | 444 | Os04g0403300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001141482.1 | 0 | 2 | 398 | 19 | 415 | hypothetical protein LOC100273593 [Zea mays] |
RefSeq | XP_002446386.1 | 0 | 1 | 398 | 18 | 415 | hypothetical protein SORBIDRAFT_06g015110 [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 | 9 | 398 | 1 | 402 | A Chain A, Structure Of Beta-Glucosidase 3b From Thermotoga Neapolitana In Complex With Alpha-D-Glucose |
PDB | 1ava_B | 0 | 9 | 398 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 9 | 398 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 9 | 398 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 9 | 398 | 2 | 404 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BU103706 | 399 | 1 | 399 | 0 |
HO780661 | 397 | 3 | 399 | 0 |
HO798064 | 370 | 3 | 372 | 0 |
JG919092 | 267 | 117 | 383 | 0 |
HO798064 | 34 | 366 | 399 | 0.00002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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