| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma02g02450.1 |
| Family | CBM45 |
| Protein Properties | Length: 897 Molecular Weight: 101816 Isoelectric Point: 5.8604 |
| Chromosome | Chromosome/Scaffold: 02 Start: 1836948 End: 1844648 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM45 | 313 | 389 | 1.4e-24 |
| LHWGVCRDDSRKWEVPPRPHPPGTVAFKERALRTQFRPRDDGKGSLALITLEEEFSGFMFVLKQNENTWFKYNGHDF | |||
| CBM45 | 120 | 206 | 1.6e-27 |
| LHWGVTYVDDVGREWDQPPRDMIPPGSILIKDYAIETPLKESSLSAEGDTLHEIRIDLKANNGIAAINFVLKDEETEAWYKNKRRDF | |||
| GH13 | 530 | 816 | 4.3e-38 |
| SELASLGFTVVWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDLVKRFHEVGIKVLGDAVLNHRCAHYQNQNGIWNIFGGPLNWDDRAVVADDPHFQG RGNKSSGDNFHAAPNIDHSQEFVRKDLKEWLCWLRKEVGYDGWRLDFVRGFWGGYVKDYIDASEPYFSVGEYWDSLSYTYSEMDHNQDAHRQRIIDWINA TNGTSGAFDVTTKGILHPALERCEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPSGKQMQGYAYILTHPGTPSVFY | |||
| Full Sequence |
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| Protein Sequence Length: 897 Download |
| MSTVALETLF PLCRRKPSFH RHKPIPLRPF FVTCSSNLND DASFIFHQQP RKTLSPVHAV 60 SHTDTSVLHS LQCPHTITNT FLINTTETVE GKIFVRLDHG KGLRDRELTV GCNLPGKWIL 120 HWGVTYVDDV GREWDQPPRD MIPPGSILIK DYAIETPLKE SSLSAEGDTL HEIRIDLKAN 180 NGIAAINFVL KDEETEAWYK NKRRDFKVSL VNNLKEDNSI IGPKWGFDLW PGNLGQISKM 240 FLQSEEADQD DSSESRVPEQ DNNQPESFCE EVPITKKVLV QNSISVSTTK CHESGAVKEL 300 LLLETDLPGD VVLHWGVCRD DSRKWEVPPR PHPPGTVAFK ERALRTQFRP RDDGKGSLAL 360 ITLEEEFSGF MFVLKQNENT WFKYNGHDFY IPLSSSSSFL NSGNKEGQSE DNSSEKIQRT 420 KSKMAQRSIF QEIERLAAEA YNIFRISIPT FSEETAAEPE VTIVEPETSI VEPQATTIVI 480 PETSVESETQ SLDPKICSGT GTGYEILCQA FNWESHKSGR WYIELKEMAS ELASLGFTVV 540 WLPPPTESVS PEGYMPKDLY NLNSRYGNID ELKDLVKRFH EVGIKVLGDA VLNHRCAHYQ 600 NQNGIWNIFG GPLNWDDRAV VADDPHFQGR GNKSSGDNFH AAPNIDHSQE FVRKDLKEWL 660 CWLRKEVGYD GWRLDFVRGF WGGYVKDYID ASEPYFSVGE YWDSLSYTYS EMDHNQDAHR 720 QRIIDWINAT NGTSGAFDVT TKGILHPALE RCEYWRLSDE KGKPPGVLGW WPSRAVTFIE 780 NHDTGSTQGH WRFPSGKQMQ GYAYILTHPG TPSVFYDHIS SHDKSEIASL ISLRKRNKIH 840 CRSRVQISKA EKDVYAAIID EKVAMKIGPG HFEPPSDSQK WSLAIEGKDY KIWEAS* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-49 | 505 | 836 | 415 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 4.0e-134 | 505 | 894 | 407 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-165 | 506 | 845 | 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 | 1.0e-176 | 503 | 894 | 398 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 1 | 896 | 928 | + alpha-amylase | ||
| Gene Ontology | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAX33231.1 | 0 | 1 | 896 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
| GenBank | AAX33233.1 | 0 | 1 | 896 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
| EMBL | CBI32016.1 | 0 | 1 | 896 | 1 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 1 | 896 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 1 | 896 | 1 | 900 | alpha-amylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2qpu_C | 0 | 504 | 894 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 504 | 894 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 504 | 894 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 504 | 894 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 504 | 894 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631183 | 936 | 1 | 897 | 0 |
| HO826981 | 403 | 495 | 897 | 0 |
| DR932783 | 288 | 505 | 792 | 0 |
| HO811991 | 299 | 599 | 897 | 0 |
| HO826981 | 30 | 432 | 459 | 1.3 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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