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Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01037695001 |
Family | GH13 |
Protein Properties | Length: 897 Molecular Weight: 103481 Isoelectric Point: 6.5833 |
Chromosome | Chromosome/Scaffold: 19 Start: 6966540 End: 7003205 |
Description | Alpha amylase family protein |
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 | 418 | 739 | 3e-26 |
TENVLPHIKEAGYNAIQLIGVVEHKDYSSVGYKVTNLYATSSRYGTPDDFKRLVDEAHGQGMLVFLDIVHSYSAADEMVGLSLFDGSNDCYFHTGKRGHH KYWGTRMFKYGDPDVLHFLLSNLNWWVVEYQIDGFQFHSLSSMIYTHNGFASFTGDLEEYCNQYVDKDALMYLILANEILHALHPKIVTIAEDATYYPGL CEPTSQGGLGFDYYVNLSAPDMWLDFLENIPDHEWSMSKIVSTLIGNRQYADKMLVYAENHNQSISGGRSFAEILFGAIKEDPLSSKTTLLRGCSLHKMI RLITLTIGGHAYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 897 Download |
MTSLSLPTQF SCHPNASSLP FSSQNRARNR VPFPKKKWRN RWRCSAAEQP QQHRTKKKKP 60 QAEADKGIDP VGFLTKLGIS HKQLSQFLRE RHKALKDLKD EIFNRHLNLQ EMASGYEILG 120 MHRNVQHRVD FMEWAPGARY CALVGDFNGW SPTENCAREG HFGRDDYGYW FIILEDKLRE 180 GEKPDELYFQ QYNYVDDNDK GDSGVTIEEL FKKANDEYWE PGEDRFIKSR YEVAAKLYEQ 240 IFGPNGPETE EELEEIPDAE TRYKAWKEQH KDDPPSNLPP FDVIDNGKEY DIYNVVDDPV 300 WREKFRAKKP PLAYWLESRK GRKAWLKKYI PGIPHGSKYR VYFNTPDGPL ERIPAWATYV 360 LPDVDGKQAF AIHWEPPPES AHRWKNMRPN VPKSLRIYEC HVGISGSEQK ISSFNEFTEN 420 VLPHIKEAGY NAIQLIGVVE HKDYSSVGYK VTNLYATSSR YGTPDDFKRL VDEAHGQGML 480 VFLDIVHSYS AADEMVGLSL FDGSNDCYFH TGKRGHHKYW GTRMFKYGDP DVLHFLLSNL 540 NWWVVEYQID GFQFHSLSSM IYTHNGFASF TGDLEEYCNQ YVDKDALMYL ILANEILHAL 600 HPKIVTIAED ATYYPGLCEP TSQGGLGFDY YVNLSAPDMW LDFLENIPDH EWSMSKIVST 660 LIGNRQYADK MLVYAENHNQ SISGGRSFAE ILFGAIKEDP LSSKTTLLRG CSLHKMIRLI 720 TLTIGGHAYL NFMGNEFGHP KRIEFPMPSN NFSLSLANRC WDLLENEVHH NLFSFDKDMM 780 KLGENERSLS RGLPNIHHVK DSAMVISYMR GPLLFIFNFH PTNSYEGYYV GVEEAGEYQI 840 ILNTDETKYG GQGLIEEGQY LRRTINRRVD GLRNCLEVSL PSRTAQVYKL SRILRI* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 3.0e-14 | 88 | 176 | 89 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 1.0e-177 | 378 | 777 | 407 | + 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. | ||
PLN03244 | PLN03244 | 0 | 1 | 896 | 902 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 0 | 1 | 896 | 903 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 331 | 888 | 576 | + 1,4-alpha-glucan-branching enzyme |
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 |
DDBJ | BAB02827.1 | 0 | 1 | 896 | 1 | 903 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 1 | 896 | 1 | 896 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 1 | 896 | 1 | 899 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002278858.1 | 0 | 1 | 896 | 1 | 866 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529457.1 | 0 | 1 | 887 | 1 | 892 | 1,4-alpha-glucan branching enzyme, 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 | 331 | 855 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 331 | 855 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 331 | 855 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
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 |
DY965821 | 293 | 261 | 553 | 0 |
JG636329 | 270 | 339 | 608 | 0 |
BF272517 | 278 | 352 | 629 | 0 |
CO104525 | 273 | 379 | 651 | 0 |
EH718768 | 263 | 357 | 619 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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