Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s526_11V6.1 |
Family | GH13 |
Protein Properties | Length: 461 Molecular Weight: 52459 Isoelectric Point: 5.9964 |
Chromosome | Chromosome/Scaffold: 526 Start: 32244 End: 36446 |
Description | alpha-amylase-like 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 82 | 372 | 1.3e-33 |
RKVSELAGWGFTSLWLPPVCDSLAPQGYLPKNLYNLNSAYGSEVELRSLLQHMKKSGLKPMADIVINHRVGSTRGKGDLYNRYDGLPMPWDEYAVSSDTG GLGKPSTGEIFKGVPNLDHSSEVVANDLKNWLEWMRKDVGFECFRFDYAKGYSPKFVKAYIEASKPRLAIGEYWDTCKYIGPNYLLDYNQDAHRQRTVDW IDGTGGLSCAFDFTTKAILQEACAKEEWYRLRDAQGRPPGLLGVWPSRAVTFIDNHDTGSTQAHWPFPRNCVAQGYAYILTHPGQPCVFYD |
Full Sequence |
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Protein Sequence Length: 461 Download |
MQDDGSESLS SSQEFAEKGK EDSAKKEVYT ERFKSIDTRV EEVEDARCDE SGEDLIRRGK 60 EIFLQGFNWE SHKQQWWRSL KRKVSELAGW GFTSLWLPPV CDSLAPQGYL PKNLYNLNSA 120 YGSEVELRSL LQHMKKSGLK PMADIVINHR VGSTRGKGDL YNRYDGLPMP WDEYAVSSDT 180 GGLGKPSTGE IFKGVPNLDH SSEVVANDLK NWLEWMRKDV GFECFRFDYA KGYSPKFVKA 240 YIEASKPRLA IGEYWDTCKY IGPNYLLDYN QDAHRQRTVD WIDGTGGLSC AFDFTTKAIL 300 QEACAKEEWY RLRDAQGRPP GLLGVWPSRA VTFIDNHDTG STQAHWPFPR NCVAQGYAYI 360 LTHPGQPCVF YDHLYEWSGD LKRVILELID IRRKLEVHSR SHITILEADT NGYSAVVDNK 420 LCVRLGNTEW TPPSDSLWEL TLSGSGYMIW SKPQPLLTSQ * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 3.0e-37 | 59 | 395 | 416 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 5.0e-124 | 61 | 452 | 410 | + alpha-amylase; Provisional | ||
PLN02784 | PLN02784 | 3.0e-146 | 27 | 452 | 437 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-156 | 62 | 401 | 343 | + 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. | ||
PLN02361 | PLN02361 | 0 | 54 | 452 | 399 | + 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 |
GenBank | AAA91884.1 | 0 | 55 | 452 | 14 | 407 | alpha-amylase [Solanum tuberosum] |
GenBank | ACV30014.1 | 0 | 55 | 452 | 14 | 407 | alpha-amylase [Solanum tuberosum] |
RefSeq | XP_001752981.1 | 0 | 53 | 453 | 4 | 403 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001785820.1 | 0 | 62 | 460 | 7 | 405 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002301935.1 | 0 | 55 | 452 | 13 | 406 | predicted protein [Populus trichocarpa] |
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 | 61 | 452 | 1 | 402 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1ava_B | 0 | 61 | 452 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 61 | 452 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 61 | 452 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 61 | 460 | 2 | 412 | 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 |
HO780661 | 398 | 55 | 452 | 0 |
HO798064 | 387 | 55 | 440 | 0 |
BU103706 | 398 | 55 | 452 | 0 |
DV704349 | 302 | 55 | 356 | 0 |
DV705742 | 299 | 55 | 353 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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