y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.002G065700.1 |
Family | CBM45 |
Protein Properties | Length: 918 Molecular Weight: 103746 Isoelectric Point: 6.163 |
Chromosome | Chromosome/Scaffold: 02 Start: 7612419 End: 7619229 |
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 | 313 | 389 | 5.3e-23 |
LHWGVCRNDTKRWEVPRSPYPPGTVPFKERALRTPLWPSPDGKGSSAQITLEEEFSGFVFVLKQNKDTWFKYLGNDF | |||
CBM45 | 119 | 205 | 1.1e-24 |
LHWGVTHVDDVGREWDQPPLDMIPPGSVPIKDYAIETPLKKSALSAEGDTLPEIRIDLKAKFGISAIHFVLKDEETGDWYKNKSRDF | |||
GH13 | 549 | 837 | 5.5e-38 |
IASELASIGFTVVWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDLVKRFHEVGIKVLGDAVLNHRCAHYQNKNGVWNIFGGCLDWDDRAVVSDDPHF QGRGNTSSGDSFHAAPNIDHSQEFVRKDLKEWLCWLRKEIGYDGWRLDFVRGFWGGYVKDYIEASEPYFAVGEYWDSLSYRNDETDYNQDAHRQRIVDWI NATKGTSGAFDVTTKGILHAALEKCEYWRLSDENGNPPGVIGWWPSRAVTFIENHDTGSTQGHWRFPSGKEMIGYAYILTHPGTPSIFY |
Full Sequence |
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Protein Sequence Length: 918 Download |
MSTVASEPLL HLCSRKPSFH SHKPIPLRPF FLPTCSSNLN DASVIFHQPR RTLSPVHAVS 60 LADTPTLHPL QCPQTITHTF EIDRTQTAVG KIFVRLDHGK DLKDWELTVR CSLPGKWILH 120 WGVTHVDDVG REWDQPPLDM IPPGSVPIKD YAIETPLKKS ALSAEGDTLP EIRIDLKAKF 180 GISAIHFVLK DEETGDWYKN KSRDFVVSLV DYIRADSDTS IIEPKRGFDF WPGNLGQISK 240 IFSKSKADEN ESSESRVPER ESNQPDGFYE EVYVTKKVLI SNSVTVSTKK CFESGAVKDI 300 LYVETDLPGD VVLHWGVCRN DTKRWEVPRS PYPPGTVPFK ERALRTPLWP SPDGKGSSAQ 360 ITLEEEFSGF VFVLKQNKDT WFKYLGNDFY VPLSSPIKLL NSSSKDDLSE GVQIEKPSQE 420 NSFFAFTDTV AYEMRNLVSD NSSDKNQKKK SKKVQQSIFE EIERLAAEAY NIFRSSIPSF 480 SKPTTAKPEA TNVEPETTIV VPEASVESEA LSLEPKICSG TGTGHEILCQ GFNWESNVSG 540 RWYMKLKEIA SELASIGFTV VWLPPPTESV SPEGYMPKDL YNLNSRYGNI DELKDLVKRF 600 HEVGIKVLGD AVLNHRCAHY QNKNGVWNIF GGCLDWDDRA VVSDDPHFQG RGNTSSGDSF 660 HAAPNIDHSQ EFVRKDLKEW LCWLRKEIGY DGWRLDFVRG FWGGYVKDYI EASEPYFAVG 720 EYWDSLSYRN DETDYNQDAH RQRIVDWINA TKGTSGAFDV TTKGILHAAL EKCEYWRLSD 780 ENGNPPGVIG WWPSRAVTFI ENHDTGSTQG HWRFPSGKEM IGYAYILTHP GTPSIFYDHI 840 FSRYKTEIAS LISLRRRNGI HCRSTVQISK AERDVYAAII DEKVAMKIGP GHFEPPSGSL 900 KWSLAIEGKH YEIWEAS* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 3.0e-48 | 523 | 857 | 421 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-136 | 526 | 915 | 407 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-161 | 527 | 866 | 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 | 2.0e-168 | 524 | 915 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 917 | 923 | + 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 | 917 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1 | 917 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1 | 917 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 917 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 917 | 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 | 525 | 915 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 525 | 915 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 525 | 915 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 525 | 915 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 525 | 915 | 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 | 929 | 1 | 918 | 0 |
HO826981 | 403 | 516 | 918 | 0 |
DR932783 | 288 | 526 | 813 | 0 |
HO811991 | 299 | 620 | 918 | 0 |
HO826981 | 33 | 461 | 491 | 4.3 |
Sequence Alignments (This image is cropped. Click for full image.) |
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