| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01020069001 |
| Family | CBM45 |
| Protein Properties | Length: 886 Molecular Weight: 99712.2 Isoelectric Point: 5.8063 |
| Chromosome | Chromosome/Scaffold: 1 Start: 10829206 End: 10842136 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM45 | 305 | 381 | 1.7e-24 |
| VHWGVCRDDSKTWEIPAAPHPPETKLFKKKALRTLLQSKEDGHGSWGLFTLDEELEGFLFVLKLNENTWLRCMGNDF | |||
| CBM45 | 117 | 203 | 8e-29 |
| LHWGVSYIDDVGSEWDQPPLEMRPPGSVAIKDYAIETPLKKLSSASERDTLHEVTIDFSPNSEIAAIRFVLKDEDYGAWYQHRGRDF | |||
| GH13 | 513 | 804 | 2e-37 |
| ELSKKVAELSSLGFTVVWLPPPTASVSPEGYMPTDLYNLNSRYGSSDELKVLVKSFHEVGVKVLGDVVLNHRCAQYQNQNGIWNIFGGRLNWDDRAIVAD DPHFQGRGNKSSGDNFHAAPNIDHSQDFVREDIKEWLCWLRKEIGYDGWRLDFVRGFWGGYVKDYMDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRI IDWINATNGAAGAFDVTTKGILHSALGRCEYWRLSDQKRKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYILTHPGTPAVF | |||
| Full Sequence |
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| Protein Sequence Length: 886 Download |
| MSTVCIEPLF QRCRRENPRF RLKSLATKPS SLNYSPKPLR NGGSFCNFKS LHGVRPLGAA 60 SIDTALFETT DVFFKETFIL KRTEVVEGKI SIRLDPGKNG ENWQLTVGCN IPGSWVLHWG 120 VSYIDDVGSE WDQPPLEMRP PGSVAIKDYA IETPLKKLSS ASERDTLHEV TIDFSPNSEI 180 AAIRFVLKDE DYGAWYQHRG RDFEVLLMDY LCEGTNTVGA KEGFGIWPGP LGQLSNMLLK 240 AEGSHPKGQD SSSVSGDLIT GFYEEHSIVK EVPVDNSVNV SVKKCPETAR NLLYLETDLI 300 GDVVVHWGVC RDDSKTWEIP AAPHPPETKL FKKKALRTLL QSKEDGHGSW GLFTLDEELE 360 GFLFVLKLNE NTWLRCMGND FYIPLLGSSS LPAQSRQGQS EGKTAGENEI VSDAAYTDGI 420 INDIRNLVSD ISSEKRQKTK TKQAQESILQ EIEKLAAEAY SIFRSSIPTF SEDAVLETLK 480 PPEKLTSGTG SGFEILCQGF NWESNKSGRW YMELSKKVAE LSSLGFTVVW LPPPTASVSP 540 EGYMPTDLYN LNSRYGSSDE LKVLVKSFHE VGVKVLGDVV LNHRCAQYQN QNGIWNIFGG 600 RLNWDDRAIV ADDPHFQGRG NKSSGDNFHA APNIDHSQDF VREDIKEWLC WLRKEIGYDG 660 WRLDFVRGFW GGYVKDYMDA SEPYFAVGEY WDSLSYTYGE MDHNQDAHRQ RIIDWINATN 720 GAAGAFDVTT KGILHSALGR CEYWRLSDQK RKPPGVVGWW PSRAVTFIEN HDTGSTQGHW 780 RFPGGKEMQG YAYILTHPGT PAVFFDHLFS HYRSEIASLI SLRNRNEIHC RSTIQITMAE 840 RDVYAAIIDE KVAMKIGPGY YEPPKGQQRW TLALEGKDYK IWETS* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 8.0e-47 | 494 | 825 | 417 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 9.0e-137 | 485 | 883 | 415 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-160 | 495 | 834 | 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 | 1.0e-168 | 491 | 883 | 399 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 1 | 885 | 899 | + 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 | AAX33233.1 | 0 | 1 | 885 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
| EMBL | CAN69906.1 | 0 | 1 | 885 | 1 | 887 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI32016.1 | 0 | 1 | 885 | 1 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 1 | 885 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 1 | 885 | 1 | 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 | 494 | 885 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 494 | 885 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 494 | 885 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 494 | 883 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 494 | 883 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631183 | 904 | 1 | 886 | 0 |
| HO826981 | 407 | 480 | 886 | 0 |
| HO811991 | 299 | 588 | 886 | 0 |
| DR932783 | 288 | 494 | 781 | 0 |
| HO826981 | 31 | 451 | 481 | 0.007 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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