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Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01033801001 |
Family | GH13 |
Protein Properties | Length: 860 Molecular Weight: 97870.1 Isoelectric Point: 5.5045 |
Chromosome | Chromosome/Scaffold: 8 Start: 17680546 End: 17724664 |
Description | starch branching enzyme 2.2 |
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 | 367 | 687 | 3.3e-28 |
LPRIKRLGYNAVQIMAIQEHSYYGSFGYHVTNFFAPSSRCGTPDDLKSLIDKAHELGLLVLMDIVHSHASNNVLDGLNRFDGTDSHYFHSGSRGYHWMWD SRLFNYGSWEVLRFLLSNARWWLDEYKFDGFRFDGVTSMMYTHHGLQVEFTGNYNEYFGYATDVDAMVYLMLVNDLIHGLFPEAVTIGEDVSGMPAFCIP VQDGGVGFDYRLHMAIADKWIELLKKPDEYWKMGDIIHTLTNRRWLEKCVAYAESHDQALVGDKTIAFWLMDKDMYEFMALDRPTTPAIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 860 Download |
MVYTLSGIRL PVVSSANNRS VLSISSGRRT ANLSLFSKKS SFSRKIFAGK SSYDSDSSSL 60 RIAASDKTLV PGSQIDGSSS STGQIEVPDT VLEDPQVLQD VDDLTMEYDN DINKPTNDCS 120 KVDENQDSVH SDLIDNDDKV QGAEKAITLS GTGTIKKEEA RPKSIPPPGT GQRIYEIDPF 180 LRGYREHLDY RFGQYKKMRE AIDKYEGGLD LFSRGYEKMG FTRSATGITY REWAPGAKSA 240 ALIGDFNNWN PNADIMTQNE FGVWEIFLPN NADGSPPIPH GSRVKIHMDT PSGIKDSIPA 300 WIEFSVQAPG EIPYNGIYYD PPEEEKYVFQ HPQPKKPKSL RIYEAHVGMS SMEPVVNTYA 360 NFRDDVLPRI KRLGYNAVQI MAIQEHSYYG SFGYHVTNFF APSSRCGTPD DLKSLIDKAH 420 ELGLLVLMDI VHSHASNNVL DGLNRFDGTD SHYFHSGSRG YHWMWDSRLF NYGSWEVLRF 480 LLSNARWWLD EYKFDGFRFD GVTSMMYTHH GLQVEFTGNY NEYFGYATDV DAMVYLMLVN 540 DLIHGLFPEA VTIGEDVSGM PAFCIPVQDG GVGFDYRLHM AIADKWIELL KKPDEYWKMG 600 DIIHTLTNRR WLEKCVAYAE SHDQALVGDK TIAFWLMDKD MYEFMALDRP TTPAIDRGIA 660 LHKMIRLITM GLGGEGYLNF MGNEFGHPEW IDFPRGDQHL PNGKRILGNN FSFDKCRRRF 720 DLGDAEYLRY RGLQEFDQAM QHLEEKYGFM TSEHQYISRK DEGDRIVVFE KGDLVFVFNF 780 HWTNSYSAYR VGCLKPGKYK IVLDSDLLLF GGFNRLDHNA EYFSSDGWYD DRPHSFLIYA 840 PCRTVVVYAP DKELEPVKG* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 4.0e-9 | 147 | 268 | 137 | + alpha-amylase | ||
PLN03244 | PLN03244 | 7.0e-134 | 276 | 812 | 543 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 63 | 859 | 801 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 323 | 738 | 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 | 276 | 848 | 577 | + 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 | ABO31358.1 | 0 | 1 | 849 | 1 | 837 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ABO31359.1 | 0 | 1 | 849 | 1 | 837 | starch branching enzyme II-2 [Malus x domestica] |
EMBL | CAA56319.1 | 0 | 1 | 858 | 1 | 854 | starch branching enzyme I [Pisum sativum] |
EMBL | CBI30261.1 | 0 | 1 | 859 | 1 | 859 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002277213.1 | 0 | 35 | 859 | 244 | 1068 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 174 | 848 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 174 | 848 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 174 | 848 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 174 | 848 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 0 | 214 | 814 | 9 | 579 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch biosynthesis | RXN-7710 | EC-2.4.1.18 | 1,4-α-glucan branching enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 690 | 168 | 857 | 0 |
HO777638 | 634 | 224 | 857 | 0 |
HO458123 | 394 | 457 | 850 | 0 |
HO458123 | 304 | 160 | 456 | 0 |
HO777638 | 47 | 177 | 223 | 0.000000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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