y
Basic Information | |
---|---|
Species | Linum usitatissimum |
Cazyme ID | Lus10016012 |
Family | GH13 |
Protein Properties | Length: 804 Molecular Weight: 91592.7 Isoelectric Point: 5.861 |
Chromosome | Chromosome/Scaffold: 172 Start: 221892 End: 226083 |
Description | starch branching enzyme 2.1 |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 247 | 578 | 1.6e-29 |
EFADNVLPRIKANNYNTVQLMAVMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLHVLMDVVHSHASNNVTDGLNGYDIGQSSQQSYFHAG EHGYHKLWDSRLFNYSNWEVLRFLLSNLRWWLEEFKFDGFRFDGVTSMLYHHHGINMAFTGHYKEYFSEATDVDAVVYLMLANCLIHDIFPDAIVIAEDV SGMPGLGRPVSEGGVGFDYRLAMAIPDKWIDYLKNKTDEEWSMKEIPGNLTNRRYTEKCVAYAESHDQSIVGDKTMAFLLMDQEMYTGMSCFDAASPRID RGIALHKMIHFLTMGLGGEGYLNFMGNEFGHP |
Full Sequence |
---|
Protein Sequence Length: 804 Download |
MLASLSLLHQ SPLCGSASLH SSPSSKISKR QSRAVSAVLT DDNRDVMTAE EDMDNIGLLS 60 GDPGLQPFRD HFKYRMKRYV EQKKLLEKHE GGLKQFAQGY LKFGFNREGD HIVYREWAPA 120 AQEAQLIGDF NGWDGSNHLM EKNEFGVWSI KLPDSGGNPA IAHSSRVKFR FKLGNGSWVD 180 RIPAWIQYAT VDPKRFGAPY DGVFWDPPAA ERYEFKYPRP PKPKAPRIYE AHGGMSASEP 240 RVNSYREFAD NVLPRIKANN YNTVQLMAVM EHSYYASFGY HVTNFFAVSS RSGTPEDLKY 300 LIDKAHSLGL HVLMDVVHSH ASNNVTDGLN GYDIGQSSQQ SYFHAGEHGY HKLWDSRLFN 360 YSNWEVLRFL LSNLRWWLEE FKFDGFRFDG VTSMLYHHHG INMAFTGHYK EYFSEATDVD 420 AVVYLMLANC LIHDIFPDAI VIAEDVSGMP GLGRPVSEGG VGFDYRLAMA IPDKWIDYLK 480 NKTDEEWSMK EIPGNLTNRR YTEKCVAYAE SHDQSIVGDK TMAFLLMDQE MYTGMSCFDA 540 ASPRIDRGIA LHKMIHFLTM GLGGEGYLNF MGNEFGHPEW IDFPREGNEW SYDKCRRQWN 600 LVDTEHLRYK FMNEFDSSMN KLDEKFSFLA SKKQIVSCTN EKDKVIVFER GDLVFVFNFH 660 PEKTYEGYKV GCDLPGKYRV ALDSDAREFG GYGRVGHDVD HFTSPEGIPG VPETNFNNRP 720 NSFKVLSPPR TCVVYYNADE SEESKSSSAA VDDVSKKLEE SGELKLVDDL QVNLDDDNVS 780 LRQKMKRAQV EKKLEEEENS SDD* 840 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-6 | 96 | 154 | 65 | + alpha-amylase | ||
PLN03244 | PLN03244 | 5.0e-131 | 159 | 735 | 582 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 33 | 737 | 705 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 211 | 616 | 406 | + 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 | 159 | 736 | 579 | + alpha-amylase |
Gene Ontology | |
---|---|
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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABN05321.1 | 0 | 3 | 744 | 44 | 780 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 9 | 789 | 38 | 825 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 13 | 765 | 52 | 816 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 13 | 765 | 29 | 793 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002510672.1 | 0 | 5 | 798 | 84 | 871 | starch branching enzyme II, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3aml_A | 0 | 46 | 751 | 1 | 706 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 46 | 743 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 46 | 743 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 46 | 743 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 8.00141e-43 | 117 | 691 | 32 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO619167 | 595 | 142 | 735 | 0 |
HO794536 | 686 | 62 | 735 | 0 |
HO777638 | 636 | 112 | 735 | 0 |
CX109187 | 382 | 355 | 736 | 0 |
HO458123 | 401 | 346 | 735 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |