| Basic Information | |
|---|---|
| Species | Cucumis sativus |
| Cazyme ID | Cucsa.285330.2 |
| Family | CBM45 |
| Protein Properties | Length: 761 Molecular Weight: 85179.8 Isoelectric Point: 6.4791 |
| Chromosome | Chromosome/Scaffold: 02653 Start: 1739563 End: 1748339 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM45 | 172 | 248 | 1.8e-22 |
| VHWGACRDDTKKWEIPAAPHPPETTVFKNKALRTLLQPKEGGKGCSGVFTIEEDFGGFLFVLKQKENSWLNYKGDDF | |||
| GH13 | 390 | 679 | 5.1e-38 |
| EKAAELSSLGFTVLWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDVVKTFHDVGIKVLGDAVLNHRCAHFKNQNGIWNIFGGRLNWDDRAVVSDDPH FQGRGNKSSGDNFHAAPNIDHSQDFVRNDIKEWLLWLRKEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVDW INATNGTAGAFDVTTKGILHSALDRCEYWRLSDEKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYLLTHPGTPSVFY | |||
| Full Sequence |
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| Protein Sequence Length: 761 Download |
| MIPPGSITIK DYAIETPLKK SSSSSSGDVH EVKIDLAPDK TIAAINFVLK DEETGIWYQH 60 KGRDFKVPLL DYCGEDGNKV GTKKGLGLWP GALGQLSNLL VKAETNSKDQ GSSSESGDTK 120 EEKKSLEGFY KELPIVKEIA VDNSISVSVR KCSETTKYLL YLESDLPGDV IVHWGACRDD 180 TKKWEIPAAP HPPETTVFKN KALRTLLQPK EGGKGCSGVF TIEEDFGGFL FVLKQKENSW 240 LNYKGDDFYI PFPSSGNLSN QQRKSKLKDT RASKISGEES EGVSVTAYTD GIIKEIRNLV 300 TDISSQKTKK KKTKEAQESI LQEIEKLAAE AYSIFRSSAP TFTEEIIETP KPVEPPVRIS 360 SGTGSGFEIL CQGFNWESHK SGRWYMELKE KAAELSSLGF TVLWLPPPTE SVSPEGYMPK 420 DLYNLNSRYG NIDELKDVVK TFHDVGIKVL GDAVLNHRCA HFKNQNGIWN IFGGRLNWDD 480 RAVVSDDPHF QGRGNKSSGD NFHAAPNIDH SQDFVRNDIK EWLLWLRKEI GYDGWRLDFV 540 RGFWGGYVKD YLDASEPYFA VGEYWDSLSY TYGEMDHNQD AHRQRIVDWI NATNGTAGAF 600 DVTTKGILHS ALDRCEYWRL SDEKGKPPGV VGWWPSRAVT FIENHDTGST QGHWRFPGGK 660 EMQGYAYLLT HPGTPSVFYD HIFSHYKSEI AALISLRKRN KVNCRSVVKI VKAERDVYAA 720 IIDETVAVKI GPGNFEPPSG SNGWSLVIEG KDYKVWEVSK * 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02784 | PLN02784 | 4.0e-8 | 94 | 253 | 168 | + alpha-amylase | ||
| PLN00196 | PLN00196 | 2.0e-138 | 359 | 757 | 416 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-165 | 369 | 708 | 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 | 6.0e-169 | 365 | 757 | 399 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 1 | 759 | 761 | + 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 | 0 | 1 | 759 | 144 | 901 | plastid alpha-amylase [Malus x domestica] |
| GenBank | AAX33231.1 | 0.001 | 112 | 252 | 62 | 213 | plastid alpha-amylase [Malus x domestica] |
| EMBL | CBI32016.1 | 0 | 1 | 759 | 138 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 1 | 759 | 145 | 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 | 368 | 757 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 368 | 757 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 368 | 757 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qps_A | 0 | 368 | 757 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 3bsg_A | 0 | 368 | 757 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631183 | 762 | 1 | 759 | 0 |
| HO826981 | 406 | 354 | 759 | 0 |
| ES805448 | 328 | 325 | 652 | 0 |
| EG631183 | 152 | 112 | 252 | 0.002 |
| HO826981 | 30 | 323 | 352 | 0.009 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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