Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000210170 |
Family | GH13 |
Protein Properties | Length: 965 Molecular Weight: 109309 Isoelectric Point: 5.9063 |
Chromosome | Chromosome/Scaffold: 018315138 Start: 2347 End: 7921 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 597 | 881 | 2.7e-37 |
LSKIGVTAVWFPPPTESVAPQGYMPSDLYNLNSSYGTVDELKHCIQEMHSHXLLALGDVVLNHRCAHKQSPNGIWNIFGGKLAWGPEAIVCDDPNFQGQG NPSSGDIFHAAPNIDHSKDFVRNDIKELLNWLRSDIGFDGWRLDFVRGFSGTYVKEYIEASVPAFAIGEYWDSLDYENGNLCYNQDAHRQRIVNWINATG GTSSAFDVTTKGILHSALHNQYWRLIDPQGKPTGVLGWWPSRAVTFLENHDTGSTQGHWPFPRDKLTQGYAYILTHPGTPVIFYD |
Full Sequence |
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Protein Sequence Length: 965 Download |
MAVGVIHRCP IASSGPHCKY DRSLCRLGRL RPLVFRTNSN REKNLFCTQH WLCKSRTSIF 60 SSMDDSNDTF TEVFDTSGSS EVLNXEEDEL VTARKGLLEA QAKQEATEKE RDQLLEELAC 120 SEGKEREYVA SILHDKELAI AGLEAAKSRF HQKLQESVEE KFSLESKLVL AKQDAVELAV 180 QVEKLAEIAF QQATSHILED ARMRVSAAET TAAEAAYQIE KQIKEVTECX ILSIVEQSKL 240 AIEKALDVAE KAGEHASKAV LEYTEGMSPL DELASLQSKN MMLQGAINDL ESQSLLTRSD 300 IDRLKLELEK AHAHANAFEL RANDAEKSLL EFQESSRKNT LQKEEEIMSL LEKMKKDSSE 360 RKKSSSKAFK AELQSIMDAI GAAKXMASAK DDAYLRRCEA LQRSLKASEA TTKMWRQRGE 420 MAESLLLKER LLGEGDEDSI YVVNGGRIDL LTDDDSLKWK LLSDGPRREI PQWMARKIRT 480 IRPRFPPRKI DVAEASSSKF RSLNLPKPDE VWSIAQEKPK EGDTLIEHVR EKETIEKKRK 540 ALEHVLERKT IQWQSTEEQT NLEPGTGTGR EIVFQGFNWE SWRRQWYLDL APKAADLSKI 600 GVTAVWFPPP TESVAPQGYM PSDLYNLNSS YGTVDELKHC IQEMHSHXLL ALGDVVLNHR 660 CAHKQSPNGI WNIFGGKLAW GPEAIVCDDP NFQGQGNPSS GDIFHAAPNI DHSKDFVRND 720 IKELLNWLRS DIGFDGWRLD FVRGFSGTYV KEYIEASVPA FAIGEYWDSL DYENGNLCYN 780 QDAHRQRIVN WINATGGTSS AFDVTTKGIL HSALHNQYWR LIDPQGKPTG VLGWWPSRAV 840 TFLENHDTGS TQGHWPFPRD KLTQGYAYIL THPGTPVIFY DHLYDFGLHD ILTELIDARR 900 RAGIHCRSSV KIYHANNEGY VAQIGDTLVM KLGDFDWNPS KENHLEGSWQ TFVDKGSDYK 960 LWVRQ |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 5.0e-43 | 571 | 901 | 421 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 6.0e-142 | 571 | 962 | 406 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-166 | 572 | 910 | 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 | 2.0e-177 | 569 | 962 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 486 | 962 | 490 | + 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 | CBI21221.1 | 0 | 2 | 965 | 10 | 975 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001782830.1 | 0 | 573 | 964 | 14 | 404 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002276872.1 | 0 | 2 | 958 | 10 | 968 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324108.1 | 0 | 574 | 965 | 10 | 401 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526120.1 | 0 | 32 | 965 | 38 | 972 | alpha-amylase, putative [Ricinus communis] |
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 | 3bsg_A | 0 | 570 | 933 | 1 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 570 | 933 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 570 | 933 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 570 | 933 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 570 | 933 | 1 | 377 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795567 | 638 | 328 | 965 | 0 |
HO778903 | 517 | 77 | 593 | 0 |
HO778903 | 105 | 593 | 697 | 0 |
HO785297 | 258 | 576 | 833 | 0 |
HO785297 | 103 | 853 | 955 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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