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Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 339218 |
Family | CBM45 |
Protein Properties | Length: 883 Molecular Weight: 99114.9 Isoelectric Point: 6.2849 |
Chromosome | Chromosome/Scaffold: 2 Start: 14032272 End: 14036740 |
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 | 127 | 210 | 3.8e-29 |
LHWGVSYVGDTGSEWDQPPEDMRPPGSIAIKDYAIETPLKKLSEGDSFFEVAINLNLESSVAALNFVLKDEETGAWYQHKGRDF | |||
GH13 | 513 | 801 | 5.8e-38 |
EKADELASLGFTVLWLPPPTESVSPEGYMPKDLYNLNSRYGTIDELKDTVRKFHKVGIKVLGDAVLNHRCAHFKNQNGVWNLFGGRLNWDDRAVVADDPH FQGRGNKSSGDNFHAAPNIDHSQDFVRKDIKEWLCWMMEEVGYDGWRLDFVRGFWGGYVKDYMDASKPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDW INATSGATGAFDVTTKGILHTALQKCEYWRLSDPKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPEGKEMQGYAYILTHPGTPAVF |
Full Sequence |
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Protein Sequence Length: 883 Download |
MSTVPIESLL HHSHLRDNSK IYRGTRSFFI PCSLNLPSHF TSNKLLHSIR TSVGASSKHR 60 RSVAIRASSS DTAVVETAQS DDVIFKENFP VQRIEKAQGK IYVRLKQVKE KNWELSVGSS 120 IPGKWILHWG VSYVGDTGSE WDQPPEDMRP PGSIAIKDYA IETPLKKLSE GDSFFEVAIN 180 LNLESSVAAL NFVLKDEETG AWYQHKGRDF KVPLVDDVPD NGNLIGAKKG FGAIGQLSNI 240 PLKQDESSAE VKKKSKSSSD STKERKGLQE FYEEMPISKR VADDNSVSVT ARKCSETSKN 300 IVSIETDLPG DVTVHWGVCK NGSKKWEIPS EPYPEDTSLF KNKALRTRLQ RKDDGNGSFG 360 LFSLDGNLEG GEDFYVPFLT SSSSLVGTEA TEAAQLSKHT PKTDKEVSAS GFTDEIITEI 420 RNLAIDIHSH KNQKTNVKEV QENILQEIEK LAAEAYSIFR STTPTFSEES ILAEAEKPDI 480 KISSGTGSGF EILCQGFNWE SHKSGRWYLE LQEKADELAS LGFTVLWLPP PTESVSPEGY 540 MPKDLYNLNS RYGTIDELKD TVRKFHKVGI KVLGDAVLNH RCAHFKNQNG VWNLFGGRLN 600 WDDRAVVADD PHFQGRGNKS SGDNFHAAPN IDHSQDFVRK DIKEWLCWMM EEVGYDGWRL 660 DFVRGFWGGY VKDYMDASKP YFAVGEYWDS LSYTYGEMDY NQDAHRQRIV DWINATSGAT 720 GAFDVTTKGI LHTALQKCEY WRLSDPKGKP PGVVGWWPSR AVTFIENHDT GSTQGHWRFP 780 EGKEMQGYAY ILTHPGTPAV FFDHIFSDYH PEIAALLSLR NRQKLHCRSE VNIDKSERDV 840 YAAIIDDKVA MKIGPGHYEP PNGSKNWSVA VEGRDYKVWE TS* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-47 | 491 | 822 | 413 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 1.0e-135 | 482 | 880 | 416 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-163 | 492 | 831 | 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 | 4.0e-171 | 488 | 880 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 882 | 904 | + 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 | AAG52558.1 | 0 | 1 | 882 | 1 | 826 | AC010675_6 putative alpha-amylase; 60344-64829 [Arabidopsis thaliana] |
GenBank | AAX33231.1 | 0 | 1 | 882 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
EMBL | CBI32016.1 | 0 | 1 | 882 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_564977.1 | 0 | 1 | 882 | 1 | 887 | AMY3 (ALPHA-AMYLASE-LIKE 3); alpha-amylase [Arabidopsis thaliana] |
RefSeq | XP_002520134.1 | 0 | 1 | 882 | 1 | 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 | 491 | 880 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 491 | 880 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 491 | 880 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 491 | 880 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 491 | 880 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 913 | 1 | 883 | 0 |
HO826981 | 407 | 477 | 883 | 0 |
GR441435 | 293 | 436 | 727 | 0 |
ES805448 | 328 | 449 | 775 | 0 |
HO826981 | 30 | 447 | 476 | 0.05 |
Sequence Alignments (This image is cropped. Click for full image.) |
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