| Basic Information | |
|---|---|
| Species | Prunus persica |
| Cazyme ID | ppa001575m |
| Family | CBM45 |
| Protein Properties | Length: 801 Molecular Weight: 91115.1 Isoelectric Point: 6.5151 |
| Chromosome | Chromosome/Scaffold: 1 Start: 26586357 End: 26594860 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM45 | 213 | 289 | 6.7e-24 |
| VHWGVCRDDSKRWEIPAAPHPPETVVFKDKALRTRLQQKEGGKGCWALFTLEEGLAGFLFVFKLNESTWLKCAGNDF | |||
| GH13 | 432 | 720 | 4.3e-38 |
| KAAELSSLGFTVIWLPPPTDSVSPEGYMPKDLYNLNSRYGNIDELKETVRTFHKVGIKVLGDAVLNHRCAEYQNQNGIWNIFGGRLNWDDRAVVADDPHF QGRGNKSSGECFHAAPNIDHSQDFVRKDIKEWLQWLREEIGYDGWRLDFVRGFWGGYVKDYIDSTEPYFAVGEYWDSLCYTYGEMDHNQDAHRQRIVDWI NATNGTAGAFDVTTKGILHAALEKCEYWRLSDQKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPHDKEMQGYAYILTHPGTPTVFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 801 Download |
| MSTVRIEPLL HYYRREKPSY RSPSKSFKLS FLNALPKKLV YNGRSFCNFQ PPTPRALTLR 60 AASTDAATVE TFESTDLFFK ETFPLKRTEV DEETGAWYQH RGRDFRVPLV DYLQEDDNVV 120 GAKWGLGAWP GALGKLSNVF VKAESSHSKD QDSSNESRDP QQKTRRVEEF YEELPIAKEI 180 SVNNSATVSV RKCPETAKNL LCLETDLPDH VVVHWGVCRD DSKRWEIPAA PHPPETVVFK 240 DKALRTRLQQ KEGGKGCWAL FTLEEGLAGF LFVFKLNEST WLKCAGNDFY IPLSSSNHSI 300 ALPREVPSED AKVPDSSTEA VQEKKFTAYT NGIINEIRNL VSDISSEKNQ KTKSKEAQES 360 ILQEIEKLAS EAYSIFRSTV PTFTEEAISE TEELKAPAKI CSGTGTGFEI LCQGFNWESH 420 KTGRWYMELQ SKAAELSSLG FTVIWLPPPT DSVSPEGYMP KDLYNLNSRY GNIDELKETV 480 RTFHKVGIKV LGDAVLNHRC AEYQNQNGIW NIFGGRLNWD DRAVVADDPH FQGRGNKSSG 540 ECFHAAPNID HSQDFVRKDI KEWLQWLREE IGYDGWRLDF VRGFWGGYVK DYIDSTEPYF 600 AVGEYWDSLC YTYGEMDHNQ DAHRQRIVDW INATNGTAGA FDVTTKGILH AALEKCEYWR 660 LSDQKGKPPG VLGWWPSRAV TFIENHDTGS TQGHWRFPHD KEMQGYAYIL THPGTPTVFY 720 DHIFSHYHSE IKALLSLRNR NKLNCRSRVK ITQAERDVYA AIIDEKVAVK IGPGHYEPPS 780 GPQRWSKSAE GRDYKVWEAS * 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02784 | PLN02784 | 4.0e-6 | 130 | 362 | 241 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 2.0e-10 | 1 | 92 | 93 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-165 | 410 | 749 | 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 | 8.0e-167 | 407 | 798 | 398 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 53 | 800 | 749 | + alpha-amylase | ||
| 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 | AAX33231.1 | 6e-25 | 1 | 92 | 1 | 93 | plastid alpha-amylase [Malus x domestica] |
| GenBank | AAX33231.1 | 0 | 91 | 800 | 195 | 901 | plastid alpha-amylase [Malus x domestica] |
| RefSeq | XP_002520134.1 | 0.0000000000001 | 1 | 92 | 1 | 93 | alpha-amylase, putative [Ricinus communis] |
| RefSeq | XP_002520134.1 | 0 | 91 | 800 | 193 | 900 | alpha-amylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2qpu_C | 0 | 409 | 798 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 409 | 798 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 409 | 798 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 409 | 798 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 409 | 798 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631183 | 712 | 91 | 801 | 0 |
| HO826981 | 403 | 399 | 801 | 0 |
| EG631183 | 96 | 1 | 92 | 1e-24 |
| HO826981 | 29 | 364 | 392 | 0.36 |
| EG631183 | 143 | 162 | 293 | 0.45 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
