y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.077550.3 |
Family | GH13 |
Protein Properties | Length: 805 Molecular Weight: 91734.2 Isoelectric Point: 4.9453 |
Chromosome | Chromosome/Scaffold: 00791 Start: 691525 End: 697618 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 243 | 568 | 6.6e-29 |
LPRIKENNYNTVQLMAIMEHSYYASFGYHITNFFAVSSRSGTPEDLKYLIDKAHGLGLRVLMDVVHSHASNNVTDGLNGFDVGQSSQDSYFHTGDRGYHK LWDSRLFNYANWEVLRFLLSNIRWWLEEYQFDGFRFDGVTSMLYHHHGINMGFSGNYNEYFSEATDVDAVVYLMLANNLTHSILPDATVIAEDVSGMPGL GRPVFEGGIGFDYRLQMAIPDKWIDYLKNKSDEEWSMGEISWNLTNRRYSEKCISYAESHDQSIVGDKTIAFLLMDKEMYSGMSCLENASPVVERGIALH KMIHFITMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 805 Download |
MSHHRQMNPF VFPYSTYKRV HSPAISSVMT EDTSTVSSTD ESMENIGILS HDPGLKPFKD 60 HFKYRVGRYT DLLNLLDKHE GGLDEFARGY LKFGFNREED GIVYREWAPA AQEAQIVGDF 120 NGWDGTNHCM EKNEFGIWSI KVYDLGGKPA ISHNSRVKFR FKHGNGVWID RIPAWIKYAT 180 VDPTKFAAPY DGVYWDPPPL ERYEFKHPRP AKPNAPRVYE AHVGMSSSEP RVNSYREFAD 240 FVLPRIKENN YNTVQLMAIM EHSYYASFGY HITNFFAVSS RSGTPEDLKY LIDKAHGLGL 300 RVLMDVVHSH ASNNVTDGLN GFDVGQSSQD SYFHTGDRGY HKLWDSRLFN YANWEVLRFL 360 LSNIRWWLEE YQFDGFRFDG VTSMLYHHHG INMGFSGNYN EYFSEATDVD AVVYLMLANN 420 LTHSILPDAT VIAEDVSGMP GLGRPVFEGG IGFDYRLQMA IPDKWIDYLK NKSDEEWSMG 480 EISWNLTNRR YSEKCISYAE SHDQSIVGDK TIAFLLMDKE MYSGMSCLEN ASPVVERGIA 540 LHKMIHFITM ALGGEGYLNF MGNEFGHPEW IDFPREGNGW SYDKCRRQWN LPDTDHLRYK 600 FLNAFDSAMN ALDEKFSFLA SSKQIVSWTG EEDKVIVFER GDLVFVFNFH PVNTYDGYKV 660 GCDLPGKYRV ALDSDASDFG GHGRVGHDID HFTSPEGIPG VPETNFNNRP NSFKILSPAR 720 TCVVYYKVDE SKEKEKDDLV GSANEDVFAR HVEEDSEGLA GCKEENDIAV GEISKTEDDD 780 IDTSKPEDDD VESNKIEDLP VRGE* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 1.0e-7 | 56 | 237 | 202 | + alpha-amylase | ||
PLN03244 | PLN03244 | 9.0e-137 | 149 | 688 | 545 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 44 | 722 | 679 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 199 | 606 | 408 | + 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 | 149 | 688 | 541 | + 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 | ABN05321.1 | 0 | 10 | 757 | 54 | 803 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 10 | 783 | 56 | 835 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 15 | 759 | 65 | 809 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 15 | 759 | 42 | 786 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002510672.1 | 0 | 21 | 764 | 113 | 856 | 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 | 3aml_A | 0 | 41 | 734 | 6 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 41 | 734 | 6 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 41 | 734 | 6 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 41 | 734 | 6 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 2.00386e-43 | 101 | 681 | 26 | 577 | 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 |
HO619167 | 592 | 132 | 722 | 0 |
HO794536 | 687 | 48 | 722 | 0 |
HO777638 | 634 | 101 | 722 | 0 |
CX109187 | 378 | 345 | 722 | 0 |
HO777638 | 46 | 52 | 97 | 0.001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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