Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 908239 |
Family | GH13 |
Protein Properties | Length: 817 Molecular Weight: 93809.5 Isoelectric Point: 5.4421 |
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 | 329 | 650 | 4.3e-29 |
LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRCGTPEELKSLIDRAHELGLVVLMDIVHSHASKNTLDGLNMFDGTDAHYFHSGPRGYHWMWD SRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLSVEFTGNYTEYFGLETDVDAVNYLMLVNDMIHALYPEAITVGEDVSGMPTFCIP VQDGGVGFDYRLHMAIADKWIEILKKRDEDWQMGDIIYTLTNRRWSEKCIAYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRPSTPLIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 817 Download |
MVVIHGVSVT PRFTIPSRPL NTSFNANSSL SFFLKKHLLS RKIFAGKQSA EFDSSSQAFA 60 ASEKVLVPDN LDDDPSSFSQ EPQIFNLESQ TMEETEALRT EDQASVFDSS YNDSKVIKER 120 GVRPRVVPPP GDGKKIYEID PMLRSYSNHL DYRYGQYKRL REEIDKYEGG LEAFSRGYEK 180 LGFSRSDAGI TYREWAPGAK AASLIGDFNN WNSNADIMTR NEFGVWEIFL PNNTDGSPAI 240 PHGSRVKIRM DTQSGIKDSI PAWIKFSVQA PGEIPFNGIY YDPPEEEKYV FKHPQPKRPK 300 SLRIYEAHVG MSSTEPMVNT YANFRDDVLP RIKRLGYNAV QIMAIQEHSY YASFGYHVTN 360 FFAPSSRCGT PEELKSLIDR AHELGLVVLM DIVHSHASKN TLDGLNMFDG TDAHYFHSGP 420 RGYHWMWDSR LFNYGSWEVL RYLLSNARWW LEEYKFDGFR FDGVTSMMYT HHGLSVEFTG 480 NYTEYFGLET DVDAVNYLML VNDMIHALYP EAITVGEDVS GMPTFCIPVQ DGGVGFDYRL 540 HMAIADKWIE ILKKRDEDWQ MGDIIYTLTN RRWSEKCIAY AESHDQALVG DKTIAFWLMD 600 KDMYDFMAVD RPSTPLIDRG IALHKMIRLI TMGLGGEGYL NFMGNEFGHP EWIDFPRGEQ 660 RLSDGSIIPG NNFSYDKCRR RFDLGDADYL RYRGLQEFDQ AMQHLEENYG FMTSEHQFIS 720 RKDEADRVIV FERGDLVFVF NFHWTSSYFD YRIGCSKPGK YKIVLDSDDP LFGGFNRLDR 780 KAEYFTYDGL YDGRPSSFMV YAPCRTAVVY ALANHD* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-9 | 144 | 230 | 93 | + alpha-amylase | ||
PLN03244 | PLN03244 | 2.0e-136 | 238 | 813 | 584 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 60 | 816 | 764 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 285 | 700 | 417 | + 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 | 238 | 813 | 580 | + 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 | AAB03100.1 | 0 | 8 | 816 | 3 | 800 | starch branching enzyme class II [Arabidopsis thaliana] |
GenBank | ABO31358.1 | 0 | 26 | 813 | 29 | 839 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ABO31359.1 | 0 | 21 | 812 | 20 | 838 | starch branching enzyme II-2 [Malus x domestica] |
RefSeq | NP_195985.3 | 0 | 1 | 816 | 1 | 805 | SBE2.2 (starch branching enzyme 2.2); 1,4-alpha-glucan branching enzyme [Arabidopsis thaliana] |
RefSeq | XP_002534111.1 | 0 | 28 | 813 | 35 | 837 | starch branching enzyme II, 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 | 3amk_A | 0 | 132 | 816 | 9 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 132 | 816 | 9 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 132 | 816 | 9 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 136 | 816 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3k1d_A | 0 | 137 | 808 | 95 | 717 | A Chain A, Crystal Structure Of Glycogen Branching Enzyme Synonym: 1,4- Glucan:1,4-Alpha-D-Glucan 6-Glucosyl-Transferase From Mycob Tuberculosis H3 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 681 | 134 | 814 | 0 |
HO777638 | 629 | 186 | 814 | 0 |
HO458123 | 393 | 419 | 811 | 0 |
HO458123 | 290 | 134 | 418 | 0 |
HO777638 | 47 | 139 | 185 | 0.000000001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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