Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi2g48150.1 |
Family | CBM45 |
Protein Properties | Length: 869 Molecular Weight: 96998 Isoelectric Point: 5.7063 |
Chromosome | Chromosome/Scaffold: 2 Start: 48454958 End: 48465714 |
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 | |||
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Family | Start | End | Evalue |
CBM45 | 299 | 375 | 2.6e-22 |
IHWGVCKDNTMTWEIPSEPHPPKTKIFRQKALQTLLQQKTDGTGNTISFLLNADYSGLVFVLKLDEYTWLRNVDNGF | |||
CBM45 | 119 | 204 | 9.5e-26 |
LHWGVSYDGEQGREWDQPPSEVRPPGSVTIKDYAIETPLVGSPNSEGHMVHEVEIKFNQDTPIAIINFVLKEEETGAWFQHKGGDF | |||
GH13 | 502 | 788 | 7.9e-36 |
KELASLGFTIVWSPPPTDSVSPEGYMPRDLYNLNSRYGTIEELKQLVNIFHEAGVKVLGDAVLNHRCAQFQNQNGVWNIFGGRINWDDRAVVADDPHFQG RGNKSSGDNFHAAPNIDHSQDFVRNDLKEWLCWMRKEVGYDGWRLDFVRGFWGGYVKDYLEASEPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWINA TSGTAGAFDVTTKGILHMALERSEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPYGMEMQGYVYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 869 Download |
MSAASWSIPA IPRAAPPARG GLPGDAFLVA ARPGPGRRRA APGRRLRLRG GGVVVARAGA 60 AEVPVTHPEE SGVVFSEKFP LRRCKTVQGK AWARVVAEPD GEGMCKIVIG CDVEGKWVLH 120 WGVSYDGEQG REWDQPPSEV RPPGSVTIKD YAIETPLVGS PNSEGHMVHE VEIKFNQDTP 180 IAIINFVLKE EETGAWFQHK GGDFRIPLSG SLEDGDPFGA QQDTVHPGAK PEGSSAQPQE 240 TVPGDKGPSV KRISEFYGEY PILKSEYVQN FVSVTVTENS ETDKSLVEFD TDITGQVIIH 300 WGVCKDNTMT WEIPSEPHPP KTKIFRQKAL QTLLQQKTDG TGNTISFLLN ADYSGLVFVL 360 KLDEYTWLRN VDNGFDFYIP LKEPHKSDEQ KVDDKSAQTD GLIGDIRNLV VGLSSRRGQR 420 AKNKVLQEDI LQEIERLAAE AYSIFRSPTI DAVEDSVYID DPATVKPACS GTGSGFEILC 480 QGFNWESHKS GKWYVELGAK AKELASLGFT IVWSPPPTDS VSPEGYMPRD LYNLNSRYGT 540 IEELKQLVNI FHEAGVKVLG DAVLNHRCAQ FQNQNGVWNI FGGRINWDDR AVVADDPHFQ 600 GRGNKSSGDN FHAAPNIDHS QDFVRNDLKE WLCWMRKEVG YDGWRLDFVR GFWGGYVKDY 660 LEASEPYFAV GEYWDSLSYT YGEMDYNQDA HRQRIVDWIN ATSGTAGAFD VTTKGILHMA 720 LERSEYWRLS DEKGKPPGVL GWWPSRAVTF IENHDTGSTQ GHWRFPYGME MQGYVYILTH 780 PGTPAVFYDH VFSHLQQDIA KLISVRRRLK IHCRSKIKIL KAEQNLYAAE IDEKVTMKIG 840 SGHFEPTGPI NWIVAVEGQD YKIWEASS* |
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 | 477 | 809 | 420 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 1.0e-133 | 477 | 865 | 406 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-158 | 478 | 817 | 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-171 | 474 | 865 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 69 | 867 | 830 | + 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 | 16 | 867 | 23 | 901 | plastid alpha-amylase [Malus x domestica] |
DDBJ | BAG89388.1 | 0 | 309 | 868 | 1 | 561 | unnamed protein product [Oryza sativa Japonica Group] |
GenBank | EEC71386.1 | 0 | 1 | 868 | 1 | 876 | hypothetical protein OsI_03507 [Oryza sativa Indica Group] |
RefSeq | NP_001044062.1 | 0 | 1 | 868 | 1 | 876 | Os01g0715400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002456247.1 | 0 | 81 | 868 | 18 | 820 | hypothetical protein SORBIDRAFT_03g032830 [Sorghum bicolor] |
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 | 477 | 865 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 477 | 865 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 477 | 865 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 477 | 865 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 477 | 865 | 2 | 403 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
Metabolic Pathways | |||
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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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 835 | 65 | 867 | 0 |
HO826981 | 403 | 466 | 867 | 0 |
GO885960 | 287 | 563 | 849 | 0 |
DV475507 | 279 | 488 | 766 | 0 |
GO859052 | 315 | 385 | 699 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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