| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 873536 |
| Family | GH13 |
| Protein Properties | Length: 904 Molecular Weight: 103789 Isoelectric Point: 6.3911 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 418 | 747 | 3.8e-24 |
| EEFTKKVLPHVKRAGYNAIQLIGIPEHKDYFTVGYRVTNFFAASSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYAAADQMVGLSLFDGSNDCYFHYGKR GHHKHWGTRMFKYGDLDVLHFLISNLNWWITEYQVDGLQFHSLASMIYTHNGFASFNNDLDDYCNQYVDRDALMYLILANEILHVLHPNIITIAEDATYY PGLCEPVSQGGLGFDYYVNLSASEMWVSLLDSVPDNEWSMSKPVLQIVSTLVANKEYADKMVSYAENHNQSISGGRSFAEILFGGVDNGSPGGKELLDRG VSLHKMIRLITFTSGGRAYLNFMGNEFGHP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 904 Download |
| MVSLSNQTRF SFHPNNLFLS ENRRLGISGV NFPRKINVKI TCFAAERPRQ EKQKKKSQSQ 60 STSDAEAGVD PVGFLTRLGI ADRIFAQFLR ERHKALKDLK DEILKRHFDF RDLASGFELL 120 GMHRHMEHRV DFMDWGPGAR YGAIIGDFNG WSPTENSARE GLFGHDDFGY WFIILEDKLR 180 EGEEPDELYF QQYNYVDDYD KGDSGVSAEE IFQKANDEYW EPGEDRFIKN RFEVPAKLYE 240 QMFGPNSPQT LEELGDIPDA ETRYKQWKEE HKNDPPRNLP PCDIIDKGQG KPYDIFNVVT 300 SPEWTKKFYE KKPPIPYWLE TRKGRKAWLK KYIPAVPHGS KYRLYFNTPD GPLERVPAWA 360 TYVQPEDEGK QAYAIHWEPS PEAAYKWKNS KPKVPKSLRI YECHVGISGS EAKISTFEEF 420 TKKVLPHVKR AGYNAIQLIG IPEHKDYFTV GYRVTNFFAA SSRYGTPDDF KRLVDEAHGL 480 GLLVFLDIVH SYAAADQMVG LSLFDGSNDC YFHYGKRGHH KHWGTRMFKY GDLDVLHFLI 540 SNLNWWITEY QVDGLQFHSL ASMIYTHNGF ASFNNDLDDY CNQYVDRDAL MYLILANEIL 600 HVLHPNIITI AEDATYYPGL CEPVSQGGLG FDYYVNLSAS EMWVSLLDSV PDNEWSMSKP 660 VLQIVSTLVA NKEYADKMVS YAENHNQSIS GGRSFAEILF GGVDNGSPGG KELLDRGVSL 720 HKMIRLITFT SGGRAYLNFM GNEFGHPERV EFPTQSNNFS FSLANRRWDL LESGVHHHLF 780 SFDKELMDLD KSKGILSRGL PSIHHVNDAN MVISFSRGPF LFIFNFHPSN SYEKYDVGVE 840 EAGEYTMILN SDEVKYGGQG LVTEDQYLQR SISKRIDGQR NCLEVFLPSR TAQVYKLTRI 900 LRI* 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02447 | PLN02447 | 6.0e-10 | 85 | 177 | 93 | + 1,4-alpha-glucan-branching enzyme | ||
| cd11321 | AmyAc_bac_euk_BE | 8.0e-175 | 381 | 784 | 411 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. | ||
| PLN02960 | PLN02960 | 0 | 1 | 903 | 903 | + alpha-amylase | ||
| PLN03244 | PLN03244 | 0 | 1 | 903 | 906 | + alpha-amylase; Provisional | ||
| PLN02447 | PLN02447 | 0 | 334 | 895 | 575 | + 1,4-alpha-glucan-branching enzyme | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| 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 |
| DDBJ | BAB02827.1 | 0 | 1 | 903 | 1 | 903 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
| EMBL | CBI26672.1 | 0 | 1 | 903 | 1 | 896 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_001154629.1 | 0 | 1 | 903 | 1 | 899 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | NP_188679.2 | 0 | 1 | 903 | 1 | 869 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | XP_002529457.1 | 0 | 4 | 894 | 5 | 892 | 1,4-alpha-glucan branching enzyme, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3amk_A | 0 | 334 | 895 | 114 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3vu2_B | 0 | 334 | 895 | 114 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 3vu2_A | 0 | 334 | 895 | 114 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BF272517 | 278 | 355 | 632 | 0 |
| CO104525 | 273 | 382 | 654 | 0 |
| DY965821 | 295 | 262 | 556 | 0 |
| JG636329 | 270 | 342 | 611 | 0 |
| DK500153 | 271 | 1 | 270 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
