y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10036717 |
Family | CBM45 |
Protein Properties | Length: 893 Molecular Weight: 100179 Isoelectric Point: 5.5557 |
Chromosome | Chromosome/Scaffold: 31 Start: 230342 End: 235044 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 305 | 381 | 1.6e-23 |
VHWGVCRDDEKNWEIPPGPHPPETIIFKEKALRTSLQSKEDGGGCSGLFTLDGDLAGFLFVLKLNDSTWLKCMGNDF | |||
CBM45 | 126 | 209 | 5.2e-27 |
LHWGVTYVDDLGSEWDQPPEHMRPSGSVPVKDYAIETPLQKASEDDPFCELKIDIDPNCAISAINFVLKDEETGTWYQYKGRDF | |||
GH13 | 524 | 811 | 2.1e-35 |
KAKDIASLGFTVVWLPPPTDSVSPEGYMPRDLYNLNSRYGNIDQLKDLVGTLHKSDIKVLGDAVLNHRCAQYQNQNGIWNMFGGRLNWDDRAVVADDPHF QGRGNKSSGDNFHAAPNIDHSQDFVRKDLKEWMCWLREEIGYDGWRLDFVRGFWGGYVKDYMDATSPDFAVGEYWDSLSYSYGEMDHNQDAHRQRIIDWI NATSGTAGAFDVTTKGILHAALERCEYWRLSDSKGKPPGVVGWWPSRAVTFVENHDTGSTQGHWRFPGGKEMQGYAYILTHPGTPAVF |
Full Sequence |
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Protein Sequence Length: 893 Download |
MSSSVTVEPL LRCHRRMEAS GFRMLTCSSS SSSAVNCPWQ KQFFRGASFR KCKLPRGSVV 60 IKASSTDTVV AETSDESSVD AFFRESFPVT RTETVEGKMF VRADQENGEG NWQLTVGCSI 120 PGNWILHWGV TYVDDLGSEW DQPPEHMRPS GSVPVKDYAI ETPLQKASED DPFCELKIDI 180 DPNCAISAIN FVLKDEETGT WYQYKGRDFK VVLGDNRLEG GNGTISSNFP GPFLYNPLLK 240 TTTQDGIGEH NDDKGEDQKL EGFYEEQTIM KHIAIKNSVS VLVRRCPETF RNLVHLETDL 300 PAVVVHWGVC RDDEKNWEIP PGPHPPETII FKEKALRTSL QSKEDGGGCS GLFTLDGDLA 360 GFLFVLKLND STWLKCMGND FYVPLSSSSS LLAQPGQEQS KDAPASERGV GANQGSGTAF 420 TDEIIKEIRH LVSGISAESS QKVKTKEAQE NILQEIEKLA AEAYSIFRSS KPTFKEEAVL 480 EEELKKKTPP LKFSGTGSGY EILLQGFNWE SHKSGRWYME FKDKAKDIAS LGFTVVWLPP 540 PTDSVSPEGY MPRDLYNLNS RYGNIDQLKD LVGTLHKSDI KVLGDAVLNH RCAQYQNQNG 600 IWNMFGGRLN WDDRAVVADD PHFQGRGNKS SGDNFHAAPN IDHSQDFVRK DLKEWMCWLR 660 EEIGYDGWRL DFVRGFWGGY VKDYMDATSP DFAVGEYWDS LSYSYGEMDH NQDAHRQRII 720 DWINATSGTA GAFDVTTKGI LHAALERCEY WRLSDSKGKP PGVVGWWPSR AVTFVENHDT 780 GSTQGHWRFP GGKEMQGYAY ILTHPGTPAV FFDHVFYSDY RSEIAALLAF RNRQKIHCRS 840 IVKIAKAERD VYAAIIDDKV AVKIGPGHFE PQNGNWKSAL EGRDYKLWEL SS* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-46 | 501 | 833 | 421 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 3.0e-137 | 501 | 889 | 405 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-163 | 502 | 842 | 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-167 | 498 | 889 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 3 | 891 | 906 | + 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 | AAX33231.1 | 0 | 3 | 891 | 2 | 901 | plastid alpha-amylase [Malus x domestica] |
EMBL | CAN69906.1 | 0 | 3 | 891 | 2 | 887 | hypothetical protein [Vitis vinifera] |
EMBL | CBI32016.1 | 0 | 3 | 891 | 2 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 3 | 891 | 2 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 3 | 891 | 2 | 900 | 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 | 2qpu_C | 0 | 500 | 889 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 500 | 889 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 500 | 889 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 500 | 889 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 500 | 889 | 1 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 906 | 3 | 891 | 0 |
HO826981 | 400 | 494 | 891 | 0 |
DR932783 | 288 | 501 | 788 | 0 |
HO811991 | 299 | 595 | 891 | 0 |
HO826981 | 20 | 455 | 474 | 0.8 |
Sequence Alignments (This image is cropped. Click for full image.) |
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