Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.G02543.1 |
Family | CBM45 |
Protein Properties | Length: 921 Molecular Weight: 103430 Isoelectric Point: 6.1533 |
Chromosome | Chromosome/Scaffold: 7 Start: 43916646 End: 43926008 |
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 | 332 | 409 | 3.4e-23 |
VHWGVCRDDSKKWEIPAAPYPPETEIFKNKALRTLLQPKEQGNGFWGSFALDEEFVGFLFVLKLKEEDVWLNCMGEDF | |||
CBM45 | 138 | 224 | 9.1e-28 |
LHWGISHVDDVGSEWDQPPAEMRPPGSIPIKDYAIETPLQKSSTSMDGDEVYEVNISIKSNSNIAAINFVLKDEESGSWYQHRGRDF | |||
GH13 | 545 | 840 | 1.7e-38 |
YKELMEKASQLASLGFTVVWLPPPTDSVSPEGYMPRDLYNLNSRYGTIDELKDLVKKFHEVNIRVLGDVVLNHRCAQYQNQNGIWNIFGGRLNWDDRAVV ADDPHFQVGRGNKSSGDNFHAAPNIDHSQDFVRKDLKEWLHWLRSEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGEMDHNQDAHR QRIIDWINATNGTAGAFDVTTKGILHAALERCEYWRLSDQKGKPPGVVGWWPSRAVTFVENHDTGSTQGHWRFPSGKEMQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 921 Download |
MSSAVSTEPL LHRSFREISR PRFRSSTLRP SPPPASLSCA PKSPSFRHAR RRCASGSGPR 60 RGGWGGAGAG ALLRVRASSS GAAVVEALES ADVLFQEAFP LQRTETAKGK IFVRLDQGKD 120 GQNWQLTVGC TLAGKWILHW GISHVDDVGS EWDQPPAEMR PPGSIPIKDY AIETPLQKSS 180 TSMDGDEVYE VNISIKSNSN IAAINFVLKD EESGSWYQHR GRDFKVPLMD SLQDDSNIVG 240 SKRGFDLWPG ALGQLSNILL KGEASDYKDK DASTDLEASK QEVRCLEGFY VEQPIVKVVS 300 IRNSVNISVK ICPKTAKTLV YLETDLPRDV IVHWGVCRDD SKKWEIPAAP YPPETEIFKN 360 KALRTLLQPK EQGNGFWGSF ALDEEFVGFL FVLKLKEEDV WLNCMGEDFY IPVSSTRSSS 420 LIRQKESDST ETSGKTMETN TEVSSTAYTD DIINEIRNLV SDISSEKSRK TKTKEAQESI 480 LQEIEKLAAE AYSIFRSSLP TFSAEAVLEQ EALEPPPHIC SGTGTGFEIL CQGFNWESNK 540 SGRWYKELME KASQLASLGF TVVWLPPPTD SVSPEGYMPR DLYNLNSRYG TIDELKDLVK 600 KFHEVNIRVL GDVVLNHRCA QYQNQNGIWN IFGGRLNWDD RAVVADDPHF QVGRGNKSSG 660 DNFHAAPNID HSQDFVRKDL KEWLHWLRSE IGYDGWRLDF VRGFWGGYVK DYLDASEPYF 720 AVGEYWDSLS YTYGEMDHNQ DAHRQRIIDW INATNGTAGA FDVTTKGILH AALERCEYWR 780 LSDQKGKPPG VVGWWPSRAV TFVENHDTGS TQGHWRFPSG KEMQGYAYIL THPGTPAVFY 840 DHIFSHYQSE IGSLISIRNR NKIHCRSTIK ITKAERDVYA AIIDDKVAMK IGPGYYEPQS 900 GPQKWSPVLE GRDYKVWETS * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 7.0e-51 | 528 | 860 | 413 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-143 | 528 | 918 | 403 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-164 | 529 | 869 | 344 | + 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 | 7.0e-170 | 526 | 918 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 79 | 920 | 843 | + 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 | 920 | 2 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 73 | 920 | 54 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 3 | 920 | 2 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 3 | 920 | 2 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 3 | 920 | 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 | 528 | 918 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 528 | 918 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 528 | 918 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 528 | 918 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 528 | 918 | 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 | 845 | 79 | 921 | 0 |
HO826981 | 408 | 514 | 921 | 0 |
ES805448 | 329 | 485 | 813 | 0 |
HO811991 | 300 | 622 | 921 | 0 |
HO826981 | 27 | 483 | 509 | 0.26 |
Sequence Alignments (This image is cropped. Click for full image.) |
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