y
Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a001104m |
Family | CBM45 |
Protein Properties | Length: 889 Molecular Weight: 99974.6 Isoelectric Point: 5.4953 |
Chromosome | Chromosome/Scaffold: 66 Start: 361189 End: 366057 |
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 | 306 | 382 | 2.4e-22 |
VHWGVCRDESKKWEIPVEPYPPGTIVFKNKALRTLLQRKNDGDGSGGSFTLGEGLLGFVFVLKLNENAWLNCKGSDF | |||
CBM45 | 125 | 211 | 3.4e-26 |
LHWGVNYVSDVGSEWDQPPLDMRPPGSIPVKDYAIETPLESKSELAEGEAFSEVAIVFDTKSSIASINFVLKDEETGRWYQHRGRDF | |||
GH13 | 518 | 806 | 6e-39 |
KASKLSELGFTVIWLPPPTDSVSPEGYMPSDLYNLNSRYGSIDQLKVLVKKLHEVGIMVLGDAVLNHRCAQFQNQNGVWNIFGGRLNWDDRAIVADDPHF QGRGNKSSGDNFHAAPNIDHSQEFVRKDIREWMNWLREEIGYDGWRLDFVRGFWGGYVKDYMESTEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVDWI NATNGTAGAFDVTTKGILHSTLERCEYWRLSDGEGKPPGVMGWWPSRAVTFIENHDTGSTQGHWRFPSGKEMQGYAYLLTHPGTPSVFY |
Full Sequence |
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Protein Sequence Length: 889 Download |
MSAVATELLF HHRVHRISPK LIPKFHLISR KSPTFNLICD TTTTDRRFVG TGLCSRYYKP 60 LKAVSSAGAA VLETSESSTI TFSETFQLER VEKVEGKITI KLDKGETEEC WQLIVGCSIP 120 GKWILHWGVN YVSDVGSEWD QPPLDMRPPG SIPVKDYAIE TPLESKSELA EGEAFSEVAI 180 VFDTKSSIAS INFVLKDEET GRWYQHRGRD FKVPLIEHPQ IDVKAGEGDV AQLTTVLVKP 240 EAAESKGDDI GGVRLQRGPL QSFYEEFSVV KETVNSNSIS VSVKHTEEKD KCVLYIETDL 300 PGDVVVHWGV CRDESKKWEI PVEPYPPGTI VFKNKALRTL LQRKNDGDGS GGSFTLGEGL 360 LGFVFVLKLN ENAWLNCKGS DFYIPLPRTV VPDKLSVSPL ISENASESNQ TSSTYTDGII 420 SEIRSLVTDI SSEKTRQTKN KKVRESILQE IEKLAAEAYS IFRSSIPTVP KIDLAEDEVL 480 EPPVKVCSGT GSGNEIVCQG FNWESHKSGN WYIELQEKAS KLSELGFTVI WLPPPTDSVS 540 PEGYMPSDLY NLNSRYGSID QLKVLVKKLH EVGIMVLGDA VLNHRCAQFQ NQNGVWNIFG 600 GRLNWDDRAI VADDPHFQGR GNKSSGDNFH AAPNIDHSQE FVRKDIREWM NWLREEIGYD 660 GWRLDFVRGF WGGYVKDYME STEPYFAVGE YWDSLSYTYG EMDHNQDAHR QRIVDWINAT 720 NGTAGAFDVT TKGILHSTLE RCEYWRLSDG EGKPPGVMGW WPSRAVTFIE NHDTGSTQGH 780 WRFPSGKEMQ GYAYLLTHPG TPSVFYDHIF SDYQNEISAL ISVRKRNTIN CRSRVTIIKA 840 ERDVYAAIVD EKLIMKIGPG HYEPTTGAEN WSVAVEGRDY KVWELTRK* 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-51 | 493 | 826 | 419 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 1.0e-136 | 488 | 884 | 410 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-164 | 496 | 835 | 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 | 7.0e-171 | 492 | 884 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 884 | 903 | + 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 | 1 | 886 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 25 | 886 | 20 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1 | 886 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_564977.1 | 0 | 1 | 886 | 1 | 887 | AMY3 (ALPHA-AMYLASE-LIKE 3); alpha-amylase [Arabidopsis thaliana] |
RefSeq | XP_002270049.1 | 0 | 1 | 886 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 494 | 884 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 494 | 884 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 494 | 884 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 494 | 884 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 494 | 884 | 1 | 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 | 886 | 0 |
HO826981 | 406 | 481 | 886 | 0 |
ES805448 | 328 | 452 | 779 | 0 |
GR072444 | 264 | 457 | 720 | 0 |
HO826981 | 29 | 450 | 476 | 0.73 |
Sequence Alignments (This image is cropped. Click for full image.) |
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