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Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 321348 |
Family | GH13 |
Protein Properties | Length: 830 Molecular Weight: 94740.5 Isoelectric Point: 5.7537 |
Chromosome | Chromosome/Scaffold: 4 Start: 17254758 End: 17260147 |
Description | starch branching enzyme 2.1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 326 | 647 | 7e-29 |
LPRIKKLGYNAVQIMAIQEHAYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELGLVVLMDIVHSHASKNTLDGLDMFDGTDGQYFHSGSRGYHWMWD SRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVEFTGNYNEYFGYSTDVDAVVYLMLVNDLIHGLYPEAIVVGEDVSGMPAFCIP VEDGGVGFDYRLHMAVADKWIELLKKRDEDWQVGDITFTLTNRRWGEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRQATPRVDRGIALHKMIR LITMGLGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 830 Download |
MVYTISGVRF PHLPSIKKNS SLPSFNEDLR RTNAVSFSLR KDSRSSGKLP LHLRSFVAIR 60 YNLGKLSLTI LSFVVLGDVD TQKTEESQET DKTCALSTSG SKSYKEDIAE MSQSLDQEVG 120 QRKIPPPGDG KKIYDIDPML NSHRTHLDYR YGQYRKLREE IDKYEGGLEA FSRGYEIFGF 180 TRSATGITYR EWAPGAKAAS LIGDFNNWNA KADVMARNDF GVWEIFLPNN ADGSSAIPHG 240 SRVKIRMDTP SGIKDSIPAW IKYSVQPPGE IPYNGVYYDP AVEDKYVFKH PRPRRPTSLR 300 IYESHVGMSS TEPKINTYAN FRDDVLPRIK KLGYNAVQIM AIQEHAYYAS FGYHVTNFFA 360 PSSRFGTPDD LKSLIDKAHE LGLVVLMDIV HSHASKNTLD GLDMFDGTDG QYFHSGSRGY 420 HWMWDSRLFN YGSWEVLRYL LSNARWWLEE YKFDGFRFDG VTSMMYTHHG LQVEFTGNYN 480 EYFGYSTDVD AVVYLMLVND LIHGLYPEAI VVGEDVSGMP AFCIPVEDGG VGFDYRLHMA 540 VADKWIELLK KRDEDWQVGD ITFTLTNRRW GEKCVVYAES HDQALVGDKT IAFWLMDKDM 600 YDFMAVDRQA TPRVDRGIAL HKMIRLITMG LGGEGYLNFM GNEFGHPEWI DFPRTDQHLP 660 DGRVIPGNNG SYDKCRRRFD LGDAEYLRYH GLQEFDRAMQ NLEETYGFMT SEHQYISRKD 720 EGDKVIVFER GNLLFVFNFH WTNSYSDYRI GCSVPGKYKI VLDSDNSLFG GFNRLDDSAE 780 FFTSDGRHDD RPCSFMVYAP CRTAVVYAAV DDDDDRSSLV PISLLPEDV* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 3.0e-10 | 150 | 227 | 84 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-136 | 236 | 803 | 577 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 65 | 803 | 743 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 283 | 697 | 416 | + 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 | 236 | 803 | 573 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
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 | AAB03099.1 | 0 | 8 | 829 | 4 | 854 | starch branching enzyme class II [Arabidopsis thaliana] |
GenBank | ABO31358.1 | 0 | 1 | 811 | 1 | 840 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ABO31359.1 | 0 | 1 | 811 | 1 | 840 | starch branching enzyme II-2 [Malus x domestica] |
EMBL | CAA56319.1 | 0 | 1 | 811 | 1 | 846 | starch branching enzyme I [Pisum sativum] |
RefSeq | NP_181180.1 | 0 | 1 | 829 | 1 | 858 | SBE2.1 (starch branching enzyme 2.1); 1,4-alpha-glucan branching enzyme [Arabidopsis thaliana] |
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 | 3amk_A | 0 | 129 | 813 | 9 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 129 | 813 | 9 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 129 | 813 | 9 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 133 | 813 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 0 | 173 | 773 | 9 | 579 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 677 | 127 | 803 | 0 |
HO777638 | 621 | 183 | 803 | 0 |
HO458123 | 388 | 416 | 803 | 0 |
HO458123 | 296 | 127 | 415 | 0 |
HO777638 | 47 | 136 | 182 | 0.0000000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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